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C I Ragan
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Articles

Mammalian inositol monophosphatase: the identification of residues important for the binding of Mg 2+ and Li + ions using fluorescence spectroscopy and site-directed mutagenesis

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M G Gore, P Greasley, G McAllister, C I Ragan
Journal: Biochemical Journal
Biochem J (1993) 296 (3): 811–815.
https://doi.org/10.1042/bj2960811
Published: 15 December 1993
View articletitled, Mammalian inositol monophosphatase: the identification of residues important for the binding of Mg 2+ and Li + ions using fluorescence spectroscopy and site-directed mutagenesis
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Articles

Bovine inositol monophosphatase. Modification, identification and mutagenesis of reactive cysteine residues

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M R Knowles, N Gee, G McAllister, C I Ragan, P J Greasley, M G Gore
Journal: Biochemical Journal
Biochem J (1992) 285 (2): 461–468.
https://doi.org/10.1042/bj2850461
Published: 15 July 1992
View articletitled, Bovine inositol monophosphatase. Modification, identification and mutagenesis of reactive cysteine residues
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Articles

cDNA cloning of human and rat brain myo -inositol monophosphatase. Expression and characterization of the human recombinant enzyme

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G McAllister, P Whiting, E A Hammond, M R Knowles, J R Atack, F J Bailey, R Maigetter, C I Ragan
Journal: Biochemical Journal
Biochem J (1992) 284 (3): 749–754.
https://doi.org/10.1042/bj2840749
Published: 15 June 1992
View articletitled, cDNA cloning of human and rat brain myo -inositol monophosphatase. Expression and characterization of the human recombinant enzyme
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Articles

Limited proteolysis and ‘ in vitro ’ mutagenesis of bovine brain inositol monophosphatase identifies an N -terminal region important for activity

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P Whiting, N S Gee, J Potter, S Howell, C I Ragan
Journal: Biochemical Journal
Biochem J (1990) 272 (2): 465–468.
https://doi.org/10.1042/bj2720465
Published: 01 December 1990
View articletitled, Limited proteolysis and ‘ in vitro ’ mutagenesis of bovine brain inositol monophosphatase identifies an N -terminal region important for activity
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Articles

Molecular size of the 5-HT 3 receptor solubilized from NCB 20 cells

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R M McKernan, C S Biggs, N Gillard, K Quirk, C I Ragan
Journal: Biochemical Journal
Biochem J (1990) 269 (3): 623–628.
https://doi.org/10.1042/bj2690623
Published: 01 August 1990
View articletitled, Molecular size of the 5-HT 3 receptor solubilized from NCB 20 cells
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Articles

Reduced inositol polyphosphate accumulation and inositol supply induced by lithium in stimulated cerebral cortex slices

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E D Kennedy, R A J Challiss, C I Ragan, S R Nahorski
Journal: Biochemical Journal
Biochem J (1990) 267 (3): 781–786.
https://doi.org/10.1042/bj2670781
Published: 01 May 1990
View articletitled, Reduced inositol polyphosphate accumulation and inositol supply induced by lithium in stimulated cerebral cortex slices
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Articles

Identification of the subunits of bovine NADH dehydrogenase which are encoded by the mitochondrial genome

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G M Gibb, C I Ragan
Journal: Biochemical Journal
Biochem J (1990) 265 (3): 903–906.
https://doi.org/10.1042/bj2650903
Published: 01 February 1990
View articletitled, Identification of the subunits of bovine NADH dehydrogenase which are encoded by the mitochondrial genome
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Articles

A monoclonal antibody to bovine brain inositol monophosphatase. Immunoaffinity purification of the brain and kidney enzymes and evidence for their structural identity

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N S Gee, S Howell, G Ryan, C I Ragan
Journal: Biochemical Journal
Biochem J (1989) 264 (3): 793–798.
https://doi.org/10.1042/bj2640793
Published: 15 December 1989
View articletitled, A monoclonal antibody to bovine brain inositol monophosphatase. Immunoaffinity purification of the brain and kidney enzymes and evidence for their structural identity
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Articles

Modification of myo -inositol monophosphatase by the arginine-specific reagent phenylglyoxal

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R G Jackson, N S Gee, C I Ragan
Journal: Biochemical Journal
Biochem J (1989) 264 (2): 419–422.
https://doi.org/10.1042/bj2640419
Published: 01 December 1989
View articletitled, Modification of myo -inositol monophosphatase by the arginine-specific reagent phenylglyoxal
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Articles

Transmembrane organization of mitochondrial NADH dehydrogenase as revealed by radiochemical labelling and cross-linking

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S D Patel, M W J Cleeter, C I Ragan
Journal: Biochemical Journal
Biochem J (1988) 256 (2): 529–535.
https://doi.org/10.1042/bj2560529
Published: 01 December 1988
View articletitled, Transmembrane organization of mitochondrial NADH dehydrogenase as revealed by radiochemical labelling and cross-linking
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Articles

Structural studies on mitochondrial NADH dehydrogenase using chemical cross-linking

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S D Patel, C I Ragan
Journal: Biochemical Journal
Biochem J (1988) 256 (2): 521–528.
https://doi.org/10.1042/bj2560521
Published: 01 December 1988
View articletitled, Structural studies on mitochondrial NADH dehydrogenase using chemical cross-linking
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Articles

Purification and properties of inositol-1,4-bisphosphatase from bovine brain

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N S Gee, G G Reid, R G Jackson, R J Barnaby, C I Ragan
Journal: Biochemical Journal
Biochem J (1988) 253 (3): 777–782.
https://doi.org/10.1042/bj2530777
Published: 01 August 1988
View articletitled, Purification and properties of inositol-1,4-bisphosphatase from bovine brain
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Articles

The purification and properties of myo -inositol monophosphatase from bovine brain

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N S Gee, C I Ragan, K J Watling, S Aspley, R G Jackson, G G Reid, D Gani, J K Shute
Journal: Biochemical Journal
Biochem J (1988) 249 (3): 883–889.
https://doi.org/10.1042/bj2490883
Published: 01 February 1988
View articletitled, The purification and properties of myo -inositol monophosphatase from bovine brain
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Articles

The dephosphorylation of inositol 1,4-bisphosphate to inositol in liver and brain involves two distinct Li + -sensitive enzymes and proceeds via inositol 4-phosphate

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C I Ragan, K J Watling, N S Gee, S Aspley, R G Jackson, G G Reid, R Baker, D C Billington, R J Barnaby, P D Leeson
Journal: Biochemical Journal
Biochem J (1988) 249 (1): 143–148.
https://doi.org/10.1042/bj2490143
Published: 01 January 1988
View articletitled, The dephosphorylation of inositol 1,4-bisphosphate to inositol in liver and brain involves two distinct Li + -sensitive enzymes and proceeds via inositol 4-phosphate
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Articles

The effect of rate limitation by cytochrome c on the redox state of the ubiquinone pool in reconstituted NADH: cytochrome c reductase

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J S Reed, C I Ragan
Journal: Biochemical Journal
Biochem J (1987) 247 (3): 657–662.
https://doi.org/10.1042/bj2470657
Published: 01 November 1987
View articletitled, The effect of rate limitation by cytochrome c on the redox state of the ubiquinone pool in reconstituted NADH: cytochrome c reductase
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Articles

Immunological analysis of plant mitochondrial NADH dehydrogenases

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I R Cottingham, M W J Cleeter, C I Ragan, A L Moore
Journal: Biochemical Journal
Biochem J (1986) 236 (1): 201–207.
https://doi.org/10.1042/bj2360201
Published: 15 May 1986
View articletitled, Immunological analysis of plant mitochondrial NADH dehydrogenases
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Articles

The polypeptide composition of the mitochondrial NADH: ubiquinone reductase complex from several mammalian species

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M W Cleeter, C I Ragan
Journal: Biochemical Journal
Biochem J (1985) 230 (3): 739–746.
https://doi.org/10.1042/bj2300739
Published: 15 September 1985
View articletitled, The polypeptide composition of the mitochondrial NADH: ubiquinone reductase complex from several mammalian species
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Articles

Chemical cross-linking of mitochondrial NADH dehydrogenase from bovine heart

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M W J Cleeter, S H Banister, C I Ragan
Journal: Biochemical Journal
Biochem J (1985) 227 (2): 467–474.
https://doi.org/10.1042/bj2270467
Published: 15 April 1985
View articletitled, Chemical cross-linking of mitochondrial NADH dehydrogenase from bovine heart
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Articles

Photoaffinity labelling of mitochondrial NADH dehydrogenase with arylazidoamorphigenin, an analogue of rotenone

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F G P Earley, C I Ragan
Journal: Biochemical Journal
Biochem J (1984) 224 (2): 525–534.
https://doi.org/10.1042/bj2240525
Published: 01 December 1984
View articletitled, Photoaffinity labelling of mitochondrial NADH dehydrogenase with arylazidoamorphigenin, an analogue of rotenone
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Articles

Cytochrome c -mediated electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase. Kinetic evidence for a mobile cytochrome c pool

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R J Froud, C I Ragan
Journal: Biochemical Journal
Biochem J (1984) 217 (2): 551–560.
https://doi.org/10.1042/bj2170551
Published: 15 January 1984
View articletitled, Cytochrome c -mediated electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase. Kinetic evidence for a mobile cytochrome c pool
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Articles

Cytochrome c mediates electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase by free diffusion along the surface of the membrane

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R J Froud, C I Ragan
Journal: Biochemical Journal
Biochem J (1984) 217 (2): 561–571.
https://doi.org/10.1042/bj2170561
Published: 15 January 1984
View articletitled, Cytochrome c mediates electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase by free diffusion along the surface of the membrane
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Articles

Properties of ubiquinol oxidase reconstituted from ubiquinol-cytochrome c reductase, cytochrome c and cytochrome c oxidase

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R J Diggens, C I Ragan
Journal: Biochemical Journal
Biochem J (1982) 202 (2): 527–534.
https://doi.org/10.1042/bj2020527
Published: 15 February 1982
View articletitled, Properties of ubiquinol oxidase reconstituted from ubiquinol-cytochrome c reductase, cytochrome c and cytochrome c oxidase
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Articles

Identification of the subunits of bovine heart mitochondrial NADH dehydrogenase that are exposed to the phospholipid bilayer by photo-labelling with 5-iodonaphth-1-yl azide

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F G P Earley, C I Ragan
Journal: Biochemical Journal
Biochem J (1980) 191 (2): 429–436.
https://doi.org/10.1042/bj1910429
Published: 01 November 1980
View articletitled, Identification of the subunits of bovine heart mitochondrial NADH dehydrogenase that are exposed to the phospholipid bilayer by photo-labelling with 5-iodonaphth-1-yl azide
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Articles

Purification and properties of l-3-glycerophosphate dehydrogenase from pig brain mitochondria

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I R Cottingham, C I Ragan
Journal: Biochemical Journal
Biochem J (1980) 192 (1): 9–18.
https://doi.org/10.1042/bj1920009
Published: 15 October 1980
View articletitled, Purification and properties of l-3-glycerophosphate dehydrogenase from pig brain mitochondria
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Articles

The reconstitution of l-3-glycerophosphate-cytochrome c oxidoreductase from l-3-glycerophosphate dehydrogenase, ubiquinone-10 and ubiquinol—cytochrome c oxidoreductase

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I R Cottingham, C I Ragan
Journal: Biochemical Journal
Biochem J (1980) 192 (1): 19–31.
https://doi.org/10.1042/bj1920019
Published: 15 October 1980
View articletitled, The reconstitution of l-3-glycerophosphate-cytochrome c oxidoreductase from l-3-glycerophosphate dehydrogenase, ubiquinone-10 and ubiquinol—cytochrome c oxidoreductase
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Articles

The organization of NADH dehydrogenase polypeptides in the inner mitochondrial membrane

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S Smith, C I Ragan
Journal: Biochemical Journal
Biochem J (1980) 185 (2): 315–326.
https://doi.org/10.1042/bj1850315
Published: 01 February 1980
View articletitled, The organization of NADH dehydrogenase polypeptides in the inner mitochondrial membrane
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Articles

An analysis of the polypeptide composition of bovine heart mitochondrial NADH-ubiquinone oxidoreductase by two-dimensional polyacrylamide-gel electrophoresis

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C Heron, S Smith, C I Ragan
Journal: Biochemical Journal
Biochem J (1979) 181 (2): 435–443.
https://doi.org/10.1042/bj1810435
Published: 01 August 1979
View articletitled, An analysis of the polypeptide composition of bovine heart mitochondrial NADH-ubiquinone oxidoreductase by two-dimensional polyacrylamide-gel electrophoresis
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Articles

The effects of lipid phase transitions on the interaction of mitochondrial NADH–ubiquinone oxidoreductase with ubiquinol–cytochrome c oxidoreductase

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C Heron, M G Gore, C I Ragan
Journal: Biochemical Journal
Biochem J (1979) 178 (2): 415–426.
https://doi.org/10.1042/bj1780415
Published: 15 February 1979
View articletitled, The effects of lipid phase transitions on the interaction of mitochondrial NADH–ubiquinone oxidoreductase with ubiquinol–cytochrome c oxidoreductase
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Articles

The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Restoration of ubiquinone-pool behaviour

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C Heron, C I Ragan, B L Trumpower
Journal: Biochemical Journal
Biochem J (1978) 174 (3): 791–800.
https://doi.org/10.1042/bj1740791
Published: 15 September 1978
View articletitled, The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Restoration of ubiquinone-pool behaviour
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Articles

The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Evidence for stoicheiometric association

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C I Ragan, C Heron
Journal: Biochemical Journal
Biochem J (1978) 174 (3): 783–790.
https://doi.org/10.1042/bj1740783
Published: 15 September 1978
View articletitled, The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Evidence for stoicheiometric association
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Articles

The role of phospholipids in the reduction of ubiquinone analogues by the mitochondrial reduced nicotinamide-adenine dinucleotide-ubiquinone oxidoreductase complex

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C I Ragan
Journal: Biochemical Journal
Biochem J (1978) 172 (3): 539–547.
https://doi.org/10.1042/bj1720539
Published: 15 June 1978
View articletitled, The role of phospholipids in the reduction of ubiquinone analogues by the mitochondrial reduced nicotinamide-adenine dinucleotide-ubiquinone oxidoreductase complex
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Articles

Specific labelling of a constituent polypeptide of bovine heart mitochondrial reduced nicotinamide-adenine dinucleotide-ubiquinone reductase by the inhibitor diphenyleneiodonium

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C I Ragan, D P Bloxham
Journal: Biochemical Journal
Biochem J (1977) 163 (3): 605–615.
https://doi.org/10.1042/bj1630605
Published: 01 June 1977
View articletitled, Specific labelling of a constituent polypeptide of bovine heart mitochondrial reduced nicotinamide-adenine dinucleotide-ubiquinone reductase by the inhibitor diphenyleneiodonium
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Articles

The interaction of reduced nicotinamide–adenine dinucleotide phosphate with reduced nicotinamide–adenine dinucleotide–ubiquinone reductase from bovine heart mitochondria

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C I Ragan
Journal: Biochemical Journal
Biochem J (1976) 158 (1): 149–151.
https://doi.org/10.1042/bj1580149
Published: 15 July 1976
View articletitled, The interaction of reduced nicotinamide–adenine dinucleotide phosphate with reduced nicotinamide–adenine dinucleotide–ubiquinone reductase from bovine heart mitochondria
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Articles

The effects of proteolytic digestion by trypsin on the structure and catalytic properties of reduced nicotinamide-adenine dinucleotide dehydrogenase from bovine heart mitochondria

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C I Ragan
Journal: Biochemical Journal
Biochem J (1976) 156 (2): 367–374.
https://doi.org/10.1042/bj1560367
Published: 15 May 1976
View articletitled, The effects of proteolytic digestion by trypsin on the structure and catalytic properties of reduced nicotinamide-adenine dinucleotide dehydrogenase from bovine heart mitochondria
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Articles

The structure and subunit composition of the particulate NADH-ubiquinone reductase of bovine heart mitochondria

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C. I Ragan
Journal: Biochemical Journal
Biochem J (1976) 154 (2): 295–305.
https://doi.org/10.1042/bj1540295
Published: 15 February 1976
View articletitled, The structure and subunit composition of the particulate NADH-ubiquinone reductase of bovine heart mitochondria
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Articles

The purification and properties of the respiratory-chain reduced nicotinamide–adenine dinucleotide dehydrogenase of Torulopsis utilis

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S. O. C. Tottmar, C. I. Ragan
Journal: Biochemical Journal
Biochem J (1971) 124 (5): 853–865.
https://doi.org/10.1042/bj1240853
Published: 01 October 1971
View articletitled, The purification and properties of the respiratory-chain reduced nicotinamide–adenine dinucleotide dehydrogenase of Torulopsis utilis
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Articles

Spectroscopic studies of flavoproteins and non-haem iron proteins of submitochondrial particles of Torulopsis utilis modified by iron- and sulphate-limited growth in continuous culture

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C. I. Ragan, P. B. Garland
Journal: Biochemical Journal
Biochem J (1971) 124 (1): 171–187.
https://doi.org/10.1042/bj1240171
Published: 01 August 1971
View articletitled, Spectroscopic studies of flavoproteins and non-haem iron proteins of submitochondrial particles of Torulopsis utilis modified by iron- and sulphate-limited growth in continuous culture
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