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C G Knight
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Articles

Thimet oligopeptidase specificity: evidence of preferential cleavage near the C-terminus and product inhibition from kinetic analysis of peptide hydrolysis

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C G Knight, P M Dando, A J Barrett
Journal: Biochemical Journal
Biochem J (1995) 308 (1): 145–150.
https://doi.org/10.1042/bj3080145
Published: 15 May 1995
View articletitled, Thimet oligopeptidase specificity: evidence of preferential cleavage near the C-terminus and product inhibition from kinetic analysis of peptide hydrolysis
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Articles

Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay

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A Anastasi, C G Knight, A J Barrett
Journal: Biochemical Journal
Biochem J (1993) 290 (2): 601–607.
https://doi.org/10.1042/bj2900601
Published: 01 March 1993
View articletitled, Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay
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Articles

A quenched fluorescent substrate for thimet peptidase containing a new fluorescent amino acid, DL-2-amino-3-(7-methoxy-4-coumaryl)propionic acid

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C G Knight
Journal: Biochemical Journal
Biochem J (1991) 274 (1): 45–48.
https://doi.org/10.1042/bj2740045
Published: 15 February 1991
View articletitled, A quenched fluorescent substrate for thimet peptidase containing a new fluorescent amino acid, DL-2-amino-3-(7-methoxy-4-coumaryl)propionic acid
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Articles

A continuous fluorimetric assay for clostridial collagenase and Pz-peptidase activity

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A J Barrett, C G Knight, M A Brown, U Tisljar
Journal: Biochemical Journal
Biochem J (1989) 260 (1): 259–263.
https://doi.org/10.1042/bj2600259
Published: 15 May 1989
View articletitled, A continuous fluorimetric assay for clostridial collagenase and Pz-peptidase activity
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Articles

Xanthene-dye-labelled phosphatidylethanolamines as probes of interfacial pH. Studies in phospholipid vesicles

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C G Knight, T Stephens
Journal: Biochemical Journal
Biochem J (1989) 258 (3): 683–687.
https://doi.org/10.1042/bj2580683
Published: 15 March 1989
View articletitled, Xanthene-dye-labelled phosphatidylethanolamines as probes of interfacial pH. Studies in phospholipid vesicles
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Articles

Dinitrophenyl-pepstatins as active-site-directed localization reagents for cathepsin D.

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I T W Matthews, R S Decker, W Hornebeck, C G Knight
Journal: Biochemical Journal
Biochem J (1983) 211 (1): 139–147.
https://doi.org/10.1042/bj2110139
Published: 01 April 1983
View articletitled, Dinitrophenyl-pepstatins as active-site-directed localization reagents for cathepsin D.
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Articles

L- trans -Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L

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A J Barrett, A A Kembhavi, M A Brown, H Kirschke, C G Knight, M Tamai, K Hanada
Journal: Biochemical Journal
Biochem J (1982) 201 (1): 189–198.
https://doi.org/10.1042/bj2010189
Published: 01 January 1982
View articletitled, L- trans -Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
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Articles

Bimane-labelled pepstatin, a fluorescent probe for the subcellular location of cathepsin D

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I T W Matthews, R S Decker, C G Knight
Journal: Biochemical Journal
Biochem J (1981) 199 (3): 611–617.
https://doi.org/10.1042/bj1990611
Published: 01 December 1981
View articletitled, Bimane-labelled pepstatin, a fluorescent probe for the subcellular location of cathepsin D
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Articles

Interaction of dinitrophenyl-pepstatins with human cathepsin D and with anti-dinitrophenyl antibody. Development of potential reagents for the localization in vivo of active proteinases at sites of tissue injury

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C G Knight, W Hornebeck, I T W Matthews, R M Hembry, J T Dingle
Journal: Biochemical Journal
Biochem J (1980) 191 (3): 835–843.
https://doi.org/10.1042/bj1910835
Published: 01 December 1980
View articletitled, Interaction of dinitrophenyl-pepstatins with human cathepsin D and with anti-dinitrophenyl antibody. Development of potential reagents for the localization in vivo of active proteinases at sites of tissue injury
Open the PDF for Interaction of dinitrophenyl-pepstatins with human cathepsin D and with anti-dinitrophenyl antibody. Development of potential reagents for the localization in vivo of active proteinases at sites of tissue injury in another window
Articles

Human cathepsin B. Application of the substrate N-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide to a study of the inhibition by leupeptin

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C G Knight
Journal: Biochemical Journal
Biochem J (1980) 189 (3): 447–453.
https://doi.org/10.1042/bj1890447
Published: 01 September 1980
View articletitled, Human cathepsin B. Application of the substrate N-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide to a study of the inhibition by leupeptin
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Articles

The accessibility of protein-bound dinitrophenyl groups to univalent fragments of anti-dinitrophenyl antibody

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C G Knight, N M Green
Journal: Biochemical Journal
Biochem J (1976) 159 (2): 323–333.
https://doi.org/10.1042/bj1590323
Published: 01 November 1976
View articletitled, The accessibility of protein-bound dinitrophenyl groups to univalent fragments of anti-dinitrophenyl antibody
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Articles

Liposomal retention of a modified anti-inflammatory steroid

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I H Shaw, C G Knight, J T Dingle
Journal: Biochemical Journal
Biochem J (1976) 158 (2): 473–476.
https://doi.org/10.1042/bj1580473
Published: 15 August 1976
View articletitled, Liposomal retention of a modified anti-inflammatory steroid
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Articles

Interaction of human cathepsin D with the inhibitor pepstatin

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C G Knight, A J Barrett
Journal: Biochemical Journal
Biochem J (1976) 155 (1): 117–125.
https://doi.org/10.1042/bj1550117
Published: 01 April 1976
View articletitled, Interaction of human cathepsin D with the inhibitor pepstatin
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Articles

The macromolecular properties of blood-group substances. Sedimentation-velocity and viscosity measurements

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J. M. Creeth, C. G. Knight
Journal: Biochemical Journal
Biochem J (1967) 105 (3): 1135–1145.
https://doi.org/10.1042/bj1051135
Published: 01 December 1967
View articletitled, The macromolecular properties of blood-group substances. Sedimentation-velocity and viscosity measurements
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