Preparation of crystalline Pseudomonas cytochrome c-551 and its general properties
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منابع مشابه
Homology of Pseudomonas cytochrome c-551 with eukaryotic c-cytochromes.
The homology of Pseudomonas cytochrome c-551 with eukaryotic cytochromes c is examined with a computer-based procedure devised to determine whether similarities exist between these proteins. One method is given by which the more recently evolved cytochromes c might have arisen from the Pseudomonas protein. This procedure involves only common genetic phenomena and accounts for most of the struct...
متن کاملThe evolutionary stability of cytochrome c-551 in Pseudomonas aeruginosa and Pseudomonas fluorescens biotype C.
Cytochrome c-551 was prepared from nine different strains of Pseudomonas aeruginosa and six of Pseudomonas fluorescens biotype C, and their amino acid sequences were compared with the sequences previously determined for the cytochromes of type strains of each species. The standard of sequence examination was such that all single amino acid substitutions, delections or insertions ought to have b...
متن کاملThe Purification and Amino Acid Composition of Pseudomonas Cytochrome C-551.
Edelman, G. M. & Benacerraf, B. (1962). Proc. nat. Acad. Sci., Wash., 48, 1035. Edelman, G. M. & Poulik, M. D. (1961). J. exp. Med. 113, 861. Eriksson, S. & Sjoquist, J. (1960). Biochim. biophys. Acta, 45, 290. Fleischman, J. B., Pain, R. H. & Porter, R. R. (1962). Arch. Biochem. Biophys. suppl. 1, 174. Fleischman, J. B., Porter, R. R. & Press, E. M. (1963). Biochem. J. 88, 220. Franklin, E. C....
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The electron-transfer reactions of cellobiose oxidase (CBO) have been investigated by conventional and by rapid-scan stopped-flow spectroscopy at pH 6.0. Analysis of the absorbance/time/wavelength matrix by Singular Value Decomposition (SVD) confirms earlier studies showing that cellobiose rapidly reduces the flavin group (7.7 s-1; cellobiose, 100 microM) which in turn slowly (0.2 s-1) reduces ...
متن کاملPseudomonas cytochrome C-551 peroxidase. A purification procedure and study of CO-binding kinetics.
A procedure is described for the purification of cytochrome c peroxidase from Pseudomonas aeruginosa involving extraction by sonication, followed by acid precipitation and chromatography on only two types of gel. The final preparation had a purity ratio A407/A280 of 4.2, and was found to be essentially pure by isoelectric focusing. The enzyme was shown to be unstable during degassing under vacu...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1960
ISSN: 0306-3283
DOI: 10.1042/bj0770194