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Articles

The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin

M P Thomas, C Verma, S M Boyd, K Brocklehurst

Biochem J (1995) 306 (1): 39–46.

https://doi.org/10.1042/bj3060039

Published: 15 February 1995

View article titled, The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin

Articles

Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain

M P Thomas, C M Topham, D Kowlessur, G W Mellor, E W Thomas, D Whitford, K Brocklehurst

Biochem J (1994) 300 (3): 805–820.

https://doi.org/10.1042/bj3000805

Published: 15 June 1994

View article titled, Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain

Articles

Some classical errors in the kinetic analysis of enzyme reactions

K Brocklehurst, C M Topham

Biochem J (1993) 295 (3): 898–899.

https://doi.org/10.1042/bj2950898

Published: 01 November 1993

View article titled, Some classical errors in the kinetic analysis of enzyme reactions

Articles

Clarification of the pH-dependent kinetic behaviour of papain by using reactivity probes and analysis of alkylation and catalysed acylation reactions in terms of multihydronic state models: implications for electrostatics calculations and interpretation of the consequences of site-specific mutations such as Asp-158-Asn and Asp-158-Glu

G W Mellor, M Patel, E W Thomas, K Brocklehurst

Biochem J (1993) 294 (1): 201–210.

https://doi.org/10.1042/bj2940201

Published: 15 August 1993

View article titled, Clarification of the pH-dependent kinetic behaviour of papain by using reactivity probes and analysis of alkylation and catalysed acylation reactions in terms of multihydronic state models: implications for electrostatics calculations and interpretation of the consequences of site-specific mutations such as Asp-158-Asn and Asp-158-Glu

Articles

Catalytic-site characteristics of the porcine calpain II 80 kDa/18 kDa heterodimer revealed by selective reaction of its essential thiol group with two-hydronic-state time-dependent inhibitors: evidence for a catalytic site Cys/His interactive system and an ionizing modulatory group

G W Mellor, S K Sreedharan, D Kowlessur, E W Thomas, K Brocklehurst

Biochem J (1993) 290 (1): 75–83.

https://doi.org/10.1042/bj2900075

Published: 15 February 1993

View article titled, Catalytic-site characteristics of the porcine calpain II 80 kDa/18 kDa heterodimer revealed by selective reaction of its essential thiol group with two-hydronic-state time-dependent inhibitors: evidence for a catalytic site Cys/His interactive system and an ionizing modulatory group

Articles

Ionization characteristics of the Cys-25/His-159 interactive system and of the modulatory group of papain: resolution of ambiguity by electronic perturbation of the quasi-2-mercaptopyridine leaving group in a new pyrimidyl disulphide reactivity probe

G W Mellor, E W Thomas, C M Topham, K Brocklehurst

Biochem J (1993) 290 (1): 289–296.

https://doi.org/10.1042/bj2900289

Published: 15 February 1993

View article titled, Ionization characteristics of the Cys-25/His-159 interactive system and of the modulatory group of papain: resolution of ambiguity by electronic perturbation of the quasi-2-mercaptopyridine leaving group in a new pyrimidyl disulphide reactivity probe

Articles

Evaluation of hydrogen-bonding and enantiomeric P 2 -S 2 hydrophobic contacts in dynamic aspects of molecular recognition by papain

M Patel, I S Kayani, W Templeton, G W Mellor, E W Thomas, K Brocklehurst

Biochem J (1992) 287 (3): 881–889.

https://doi.org/10.1042/bj2870881

Published: 01 November 1992

View article titled, Evaluation of hydrogen-bonding and enantiomeric P 2 -S 2 hydrophobic contacts in dynamic aspects of molecular recognition by papain

Articles

Polyclonal antibody-catalysed amide hydrolysis

G Gallacher, M Searcey, C S Jackson, K Brocklehurst

Biochem J (1992) 284 (3): 675–680.

https://doi.org/10.1042/bj2840675

Published: 15 June 1992

View article titled, Polyclonal antibody-catalysed amide hydrolysis

Articles

In defence of the general validity of the Cha method of deriving rate equations. The importance of explicit recognition of the thermodynamic box in enzyme kinetics

C M Topham, K Brocklehurst

Biochem J (1992) 282 (1): 261–265.

https://doi.org/10.1042/bj2820261

Published: 15 February 1992

View article titled, In defence of the general validity of the Cha method of deriving rate equations. The importance of explicit recognition of the thermodynamic box in enzyme kinetics

Articles

Variation in the P 2 -S 2 stereochemical selectivity towards the enantiomeric N -acetylphenylalanylglycine 4-nitroanilides among the cysteine proteinases papain, ficin and actinidin

M Patel, I S Kayani, G W Mellor, S Sreedharan, W Templeton, E W Thomas, M Thomas, K Brocklehurst

Biochem J (1992) 281 (2): 553–559.

https://doi.org/10.1042/bj2810553

Published: 15 January 1992

View article titled, Variation in the P 2 -S 2 stereochemical selectivity towards the enantiomeric N -acetylphenylalanylglycine 4-nitroanilides among the cysteine proteinases papain, ficin and actinidin

Articles

Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase Ω. Three-dimensional structure of papaya proteinase Ω deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis

C M Topham, E Salih, C Frazao, D Kowlessur, J P Overington, M Thomas, S M Brocklehurst, M Patel, E W Thomas, K Brocklehurst

Biochem J (1991) 280 (1): 79–92.

https://doi.org/10.1042/bj2800079

Published: 15 November 1991

View article titled, Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase Ω. Three-dimensional structure of papaya proteinase Ω deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis

Articles

A polyclonal antibody preparation with Michaelian catalytic properties

G Gallacher, C S Jackson, M Searcey, G T Badman, R Goel, C M Topham, G W Mellor, K Brocklehurst

Biochem J (1991) 279 (3): 871–881.

https://doi.org/10.1042/bj2790871

Published: 01 November 1991

View article titled, A polyclonal antibody preparation with Michaelian catalytic properties

Articles

Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics

K Brocklehurst, C M Topham

Biochem J (1990) 270 (2): 561–563.

https://doi.org/10.1042/bj2700561

Published: 01 September 1990

View article titled, Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics

Articles

A re-appraisal of the structural basis of stereochemical recognition in papain. Insensitivity of binding-site-catalytic-site signalling to P 2 -chirality in a time-dependent inhibition

W Templeton, D Kowlessur, E W Thomas, C M Topham, K Brocklehurst

Biochem J (1990) 266 (3): 645–651.

https://doi.org/10.1042/bj2660645

Published: 15 March 1990

View article titled, A re-appraisal of the structural basis of stereochemical recognition in papain. Insensitivity of binding-site-catalytic-site signalling to P 2 -chirality in a time-dependent inhibition

Articles

Dependence of the P 2 -S 2 stereochemical selectivity of papain on the nature of the catalytic-site chemistry. Quantification of selectivity in the catalysed hydrolysis of the enantiomeric N -acetylphenylalanylglycine 4-nitroanilides

D Kowlessur, E W Thomas, C M Topham, W Templeton, K Brocklehurst

Biochem J (1990) 266 (3): 653–660.

https://doi.org/10.1042/bj2660653

Published: 15 March 1990

View article titled, Dependence of the P 2 -S 2 stereochemical selectivity of papain on the nature of the catalytic-site chemistry. Quantification of selectivity in the catalysed hydrolysis of the enantiomeric N -acetylphenylalanylglycine 4-nitroanilides

Articles

The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain

D Kowlessur, M O'Driscoll, C M Topham, W Templeton, E W Thomas, K Brocklehurst

Biochem J (1989) 259 (2): 443–452.

https://doi.org/10.1042/bj2590443

Published: 15 April 1989

View article titled, The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain

Articles

Identification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papain

D Kowlessur, C M Topham, E W Thomas, M O'Driscoll, W Templeton, K Brocklehurst

Biochem J (1989) 258 (3): 755–764.

https://doi.org/10.1042/bj2580755

Published: 15 March 1989

View article titled, Identification of signalling and non-signalling binding contributions to enzyme reactivity. Alternative combinations of binding interactions provide for change in transition-state geometry in reactions of papain

Articles

The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain

K Brocklehurst, M O'Driscoll, D Kowlessur, I R Phillips, W Templeton, E W Thomas, C M Topham, C W Wharton

Biochem J (1989) 257 (1): 309–310.

https://doi.org/10.1042/bj2570309

Published: 01 January 1989

View article titled, The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain

Articles

Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics

K Brocklehurst, S M Brocklehurst, D Kowlessur, M O'Driscoll, G Patel, E Salih, W Templeton, E Thomas, C M Topham, F Willenbrock

Biochem J (1988) 256 (2): 543–558.

https://doi.org/10.1042/bj2560543

Published: 01 December 1988

View article titled, Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics

Articles

Consequences of molecular recognition in the S 1 -S 2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P 1 -P 2 amide bond into a two-protonic-state reactivity probe

K Brocklehurst, D Kowlessur, G Patel, W Templeton, K Quigley, E W Thomas, C W Wharton, F Willenbrock, R J Szawelski

Biochem J (1988) 250 (3): 761–772.

https://doi.org/10.1042/bj2500761

Published: 15 March 1988

View article titled, Consequences of molecular recognition in the S 1 -S 2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P 1 -P 2 amide bond into a two-protonic-state reactivity probe

Articles

pH-activity curves for enzyme-catalysed reactions in which the hydron is a product or reactant

H B F Dixon, K Brocklehurst, K F Tipton

Biochem J (1987) 248 (2): 573–578.

https://doi.org/10.1042/bj2480573

Published: 01 December 1987

View article titled, pH-activity curves for enzyme-catalysed reactions in which the hydron is a product or reactant

Articles

Differences in the chemical and catalytic characteristics of two crystallographically ‘identical’ enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment

E Salih, J P G Malthouse, D Kowlessur, M Jarvis, M O'Driscoll, K Brocklehurst

Biochem J (1987) 247 (1): 181–193.

https://doi.org/10.1042/bj2470181

Published: 01 October 1987

View article titled, Differences in the chemical and catalytic characteristics of two crystallographically ‘identical’ enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment

Articles

Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding

K Brocklehurst, D Kowlessur, M O'Driscoll, G Patel, S Quenby, E Salih, W Templeton, E W Thomas, F Willenbrock

Biochem J (1987) 244 (1): 173–181.

https://doi.org/10.1042/bj2440173

Published: 15 May 1987

View article titled, Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding

Articles

Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites

F Willenbrock, K Brocklehurst

Biochem J (1986) 238 (1): 103–107.

https://doi.org/10.1042/bj2380103

Published: 15 August 1986

View article titled, Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites

Articles

Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives

B S Baines, K Brocklehurst, P R Carey, M Jarvis, E Salih, A C Storer

Biochem J (1986) 233 (1): 119–129.

https://doi.org/10.1042/bj2330119

Published: 01 January 1986

View article titled, Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives

Articles

Fresh non-fruit latex of Carica papaya contains papain, multiple forms of chymopapain A and papaya proteinase Ω

K Brocklehurst, E Salih, R McKee, H Smith

Biochem J (1985) 228 (2): 525–527.

https://doi.org/10.1042/bj2280525

Published: 01 June 1985

View article titled, Fresh non-fruit latex of Carica papaya contains papain, multiple forms of chymopapain A and papaya proteinase Ω

Articles

Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4

F Willenbrock, K Brocklehurst

Biochem J (1985) 227 (2): 511–519.

https://doi.org/10.1042/bj2270511

Published: 15 April 1985

View article titled, Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4

Articles

A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and −161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide catalysed by cathepsin B and of l-arginine 2-naphthylamide catalysed by cathepsin H.

F Willenbrock, K Brocklehurst

Biochem J (1985) 227 (2): 521–528.

https://doi.org/10.1042/bj2270521

Published: 15 April 1985

View article titled, A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and −161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide catalysed by cathepsin B and of l-arginine 2-naphthylamide catalysed by cathepsin H.

Articles

Comparative resonance Raman spectroscopic and kinetic studies of acyl-enzymes involving papain, actinidin and papaya peptidase II

K Brocklehurst, P R Carey, H H Lee, E Salih, A C Storer

Biochem J (1984) 223 (3): 649–657.

https://doi.org/10.1042/bj2230649

Published: 01 November 1984

View article titled, Comparative resonance Raman spectroscopic and kinetic studies of acyl-enzymes involving papain, actinidin and papaya peptidase II

Articles

Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2′-dipyridyl disulphide) and with a specific synthetic substrate (N-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide)

F Willenbrock, K Brocklehurst

Biochem J (1984) 222 (3): 805–814.

https://doi.org/10.1042/bj2220805

Published: 15 September 1984

View article titled, Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2′-dipyridyl disulphide) and with a specific synthetic substrate (N-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide)

Articles

‘Chymopapain S‘ is chymopapain A

K Brocklehurst, B S Baines, E Salih, C Hatzoulis

Biochem J (1984) 221 (2): 553–554.

https://doi.org/10.1042/bj2210553

Published: 15 July 1984

View article titled, ‘Chymopapain S‘ is chymopapain A

Articles

Differences between the electric fields of the catalytic sites of papain and actinidin detected by using the thiol-located nitrobenzofurazan label as a spectroscopic reporter group

K Brocklehurst, E Salih, T S Lodwig

Biochem J (1984) 220 (2): 609–612.

https://doi.org/10.1042/bj2200609

Published: 01 June 1984

View article titled, Differences between the electric fields of the catalytic sites of papain and actinidin detected by using the thiol-located nitrobenzofurazan label as a spectroscopic reporter group

Articles

Investigation of the catalytic site of actinidin by using benzofuroxan as a reactivity probe with selectivity for the thiolate-imidazolium ion-pair systems of cysteine proteinases. Evidence that the reaction of the ion-pair of actinidin (p K I 3.0, p K II 9.6) is modulated by the state of ionization of a group associated with a molecular p K a of 5.5

E Salih, K Brocklehurst

Biochem J (1983) 213 (3): 713–718.

https://doi.org/10.1042/bj2130713

Published: 01 September 1983

View article titled, Investigation of the catalytic site of actinidin by using benzofuroxan as a reactivity probe with selectivity for the thiolate-imidazolium ion-pair systems of cysteine proteinases. Evidence that the reaction of the ion-pair of actinidin (p K I 3.0, p K II 9.6) is modulated by the state of ionization of a group associated with a molecular p K a of 5.5

Articles

A re-evaluation of the nomenclature of the cysteine proteinases of Carica papaya and a rational basis for their identification

K Brocklehurst, E Salih

Biochem J (1983) 213 (2): 559–560.

https://doi.org/10.1042/bj2130559

Published: 01 August 1983

View article titled, A re-evaluation of the nomenclature of the cysteine proteinases of Carica papaya and a rational basis for their identification

Articles

Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme p K a variability in reactions of papain for its catalytic mechanism

K Brocklehurst, S J F Willenbrock, E Salih

Biochem J (1983) 211 (3): 701–708.

https://doi.org/10.1042/bj2110701

Published: 01 June 1983

View article titled, Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme p K a variability in reactions of papain for its catalytic mechanism

Articles

A marked gradation in active-centre properties in the cysteine proteinases revealed by neutral and anionic reactivity probes. Reactivity characteristics of the thiol groups of actinidin, ficin, papain and papaya peptidase A towards 4,4′-dipyridyl disulphide and 5,5′-dithiobis-(2-nitrobenzoate) dianion

K Brocklehurst, S M Mushiri, G Patel, F Willenbrock

Biochem J (1983) 209 (3): 873–879.

https://doi.org/10.1042/bj2090873

Published: 01 March 1983

View article titled, A marked gradation in active-centre properties in the cysteine proteinases revealed by neutral and anionic reactivity probes. Reactivity characteristics of the thiol groups of actinidin, ficin, papain and papaya peptidase A towards 4,4′-dipyridyl disulphide and 5,5′-dithiobis-(2-nitrobenzoate) dianion

Articles

Characterization of papaya peptidase A as a cysteine proteinase of Carica papaya L. with active-centre properties that differ from those of papain by using 2,2′-dipyridyl disulphide and 4-chloro-7-nitrobenzofurazan as reactivity probes. Use of two-protonic-state electrophiles in the identification of catalytic-site thiol groups

B S Baines, K Brocklehurst

Biochem J (1982) 205 (1): 205–211.

https://doi.org/10.1042/bj2050205

Published: 01 July 1982

View article titled, Characterization of papaya peptidase A as a cysteine proteinase of Carica papaya L. with active-centre properties that differ from those of papain by using 2,2′-dipyridyl disulphide and 4-chloro-7-nitrobenzofurazan as reactivity probes. Use of two-protonic-state electrophiles in the identification of catalytic-site thiol groups

Articles

Evidence for a close similarity in the catalytic sites of papain and ficin in near-neutral media despite differences in acidic and alkaline media. Kinetics of the reactions of papain and ficin with chloroacetate

K Brocklehurst, S M Mushiri, G Patel, F Willenbrock

Biochem J (1982) 201 (1): 101–104.

https://doi.org/10.1042/bj2010101

Published: 01 January 1982

View article titled, Evidence for a close similarity in the catalytic sites of papain and ficin in near-neutral media despite differences in acidic and alkaline media. Kinetics of the reactions of papain and ficin with chloroacetate

Articles

Differences in the interaction of the catalytic groups of the active centres of actinidin and papain Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes

K Brocklehurst, B S Baines, J P Malthouse

Biochem J (1981) 197 (3): 739–746.

https://doi.org/10.1042/bj1970739

Published: 01 September 1981

View article titled, Differences in the interaction of the catalytic groups of the active centres of actinidin and papain Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes

Articles

Evidence that the lack of high catalytic activity of thiolsubtilisin towards specific substrates may be due to an inappropriately located proton-distribution system. Demonstration of highly nucleophilic character of the thiol group of thiolsubtilisin in the catalytically relevant ionization state of the active centre by use of a two-protonic-state reactivity probe

K Brocklehurst, J P G Malthouse

Biochem J (1981) 193 (3): 819–823.

https://doi.org/10.1042/bj1930819

Published: 01 March 1981

View article titled, Evidence that the lack of high catalytic activity of thiolsubtilisin towards specific substrates may be due to an inappropriately located proton-distribution system. Demonstration of highly nucleophilic character of the thiol group of thiolsubtilisin in the catalytically relevant ionization state of the active centre by use of a two-protonic-state reactivity probe

Articles

Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin

K Brocklehurst, J P G Malthouse

Biochem J (1980) 191 (3): 707–718.

https://doi.org/10.1042/bj1910707

Published: 01 December 1980

View article titled, Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin

Articles

Evidence that the active centre of chymopapain A is different from the active centres of some other cysteine proteinases and that the Brønsted coefficient (β nuc. ) for the reactions of thiolate anions with 2,2′-dipyridyl disulphide may be decreased by reagent protonation

K Brocklehurst, B S Baines, M S Mushiri

Biochem J (1980) 189 (1): 189–192.

https://doi.org/10.1042/bj1890189

Published: 01 July 1980

View article titled, Evidence that the active centre of chymopapain A is different from the active centres of some other cysteine proteinases and that the Brønsted coefficient (β nuc. ) for the reactions of thiolate anions with 2,2′-dipyridyl disulphide may be decreased by reagent protonation

Articles

A kinetic method for the study of solvent environments of thiol groups in proteins involving the use of a pair of isomeric reactivity probes and a differential solvent effect. Investigation of the active centre of ficin by using 2,2'- and 4,4'- dipyridyl disulphides as reactivity probes

J P G Malthouse, K Brocklehurst

Biochem J (1980) 185 (1): 217–222.

https://doi.org/10.1042/bj1850217

Published: 01 January 1980

View article titled, A kinetic method for the study of solvent environments of thiol groups in proteins involving the use of a pair of isomeric reactivity probes and a differential solvent effect. Investigation of the active centre of ficin by using 2,2'- and 4,4'- dipyridyl disulphides as reactivity probes

Articles

Reactivities of neutral and cationic forms of 2,2′-dipyridyl disulphide towards thiolate anions. Detection of differences between the active centres of actinidin, papain and ficin by a three-protonic-state reactivity probe

K Brocklehurst, T Stuchbury, J P G Malthouse

Biochem J (1979) 183 (2): 233–238.

https://doi.org/10.1042/bj1830233

Published: 01 November 1979

View article titled, Reactivities of neutral and cationic forms of 2,2′-dipyridyl disulphide towards thiolate anions. Detection of differences between the active centres of actinidin, papain and ficin by a three-protonic-state reactivity probe

Articles

Evidence for association-activation effects in reactions of papain from studies on its reactivity towards isomeric two-protonic-state reactivity probes

K Brocklehurst, J A L Herbert, R Norris, H Suschitzky

Biochem J (1979) 183 (2): 369–373.

https://doi.org/10.1042/bj1830369

Published: 01 November 1979

View article titled, Evidence for association-activation effects in reactions of papain from studies on its reactivity towards isomeric two-protonic-state reactivity probes

Articles

The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions

K Brocklehurst

Biochem J (1979) 181 (3): 775–778.

https://doi.org/10.1042/bj1810775

Published: 01 September 1979

View article titled, The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions

Articles

A thiol-labelling reagent and reactivity probe containing electrophilic mercury and a chromophoric leaving group

B S Baines, K Brocklehurst

Biochem J (1979) 179 (3): 701–704.

https://doi.org/10.1042/bj1790701

Published: 01 June 1979

View article titled, A thiol-labelling reagent and reactivity probe containing electrophilic mercury and a chromophoric leaving group

Articles

Mechanism of the reaction of papain with substrate-derived diazomethyl ketones. Implications for the difference in site specificity of halomethyl ketones for serine proteinases and cysteine proteinases and for stereoelectronic requirements in the papain catalytic mechanism

K Brocklehurst, J P G Malthouse

Biochem J (1978) 175 (2): 761–764.

https://doi.org/10.1042/bj1750761

Published: 01 November 1978

View article titled, Mechanism of the reaction of papain with substrate-derived diazomethyl ketones. Implications for the difference in site specificity of halomethyl ketones for serine proteinases and cysteine proteinases and for stereoelectronic requirements in the papain catalytic mechanism

Articles

A spectrophotometric method for the detection of contaminant chymopapains in preparations of papain. Selective modification of one type of thiol group in the chymopapains by a two-protonic-state reagent

B S Baines, K Brocklehurst

Biochem J (1978) 173 (1): 345–347.

https://doi.org/10.1042/bj1730345

Published: 01 July 1978

View article titled, A spectrophotometric method for the detection of contaminant chymopapains in preparations of papain. Selective modification of one type of thiol group in the chymopapains by a two-protonic-state reagent

Articles

The pH-dependence of second-order rate constants of enzyme modification may provide free-reactant p K a values

K Brocklehurst, H B F Dixon

Biochem J (1977) 167 (3): 859–862.

https://doi.org/10.1042/bj1670859

Published: 01 December 1977

View article titled, The pH-dependence of second-order rate constants of enzyme modification may provide free-reactant p K a values

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