The Purification and Amino Acid Composition of Pseudomonas Cytochrome C-551.
نویسنده
چکیده
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. (1962). Nature, Lond., 195, 393. Franklin, E. C., Fudenberg, H., Meltzer, M. & Stanworth, D. R. (1962). Proc. nat. Acad. Sci., Wash., 48, 914. Franklin, E. C. & Stanworth, D. R. (1961). J. exp. Med. 114, 521. Harboe, M., Osterland, C. K. & Kunkel, H. G. (1962a). Science, 136, 979. Harboe, M., Osterland, C. K., Mannik, M. & Kunkel, H. G. (1962b). J. exp. Med. 116, 719. Heremans, J. F. & Heremans, M. Th. (1961). Acta med. scand. 170 (suppl. 367), 27. Korngold, L. & Lipari, R. (1956). Cancer, 9, 183. Mannik, M. & Kunkel, H. G. (1962). J. exp. Med. 116, 859. Mannik, M. & Kunkel, H. G. (1963). J. exp. Med. 117, 213. Olins, D. E. & Edelman, G. M. (1962). J. exp. Med. 116, 635. Ouchterlony, 0. (1953). Acta path. microbiol. scand. 32, 231. Pain, R. H. (1963). Biochem. J. 88, 234. Peterson, E. A. & Sober, H. A. (1956). J. Amer. chem. Soc. 78, 751. Porath, J. (1956). Biochim. biophys. Acta, 22, 151. Porter, R. R. (1957). In Methods in Enzymology, vol. 4, p. 221. Ed. by Colowick, S. P. & Kaplan, N. 0. Nem York: Academic Press Inc. Porter, R. R. (1959). Biochem. J. 73, 119. Porter, R. R. (1962). In Symposium on Basic Problems in Neoplastic Disease, p. 117. Ed. by Gellhorn, A. & Hirschberg, E. Columbia University Press. Poulik, M. D. & Edelman, G. M. (1961). Nature, Lond., 191, 1274. Scheidegger, J. J. (1955). Int. Arch. Allergy, N.Y., 7, 103. Sober, H. A. & Peterson, E. A. (1958). Fed. Proc. 17, 1116.
منابع مشابه
Amino acid sequence of cytochrome c-552 from a thermophilic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus.
The complete amino acid sequence of cytochrome c-552 from an extremely thermophilic hydrogen bacterium, Hydrogenobacter thermophilus TK-6 (IAM 12695), was determined. It is a single polypeptide chain of 80 residues, and its molecular weight, including heme, was calculated to be 7,599. The sequence of cytochrome c-552 from H. thermophilus TK-6 closely resembles that of cytochromes c-551 from Pse...
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 کاملA comparison of the physical and chemical properties of four cytochromes c from Azotobacter vinelandii.
1. A modified method for the separation and purification of four cytochromes c from Azotobacter vinelandii is described. Two new cytochromes c have been purified and are designated cytochromes c(551) and c(555). 2. Additional evidence is presented to establish the dihaem nature of cytochrome c(4). Ultracentrifugation data indicated similar molecular weights for the native and the denatured prot...
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...
متن کاملStabilization mechanism of cytochrome c552 from a moderately thermophilic bacterium, Hydrogenophilus thermoluteolus.
Cytochrome c(552) (PH c(552)) from moderately thermophilic Hydrogenophilus thermoluteolus exhibits stability intermediate between those of cytochrome c(552) (HT c(552)) from thermophilic Hydrogenobacter thermophilus and cytochrome c(551) (PA c(551)) from mesophilic Pseudomonas aeruginosa. To understand the mechanism of stabilization of PH c(552), we introduced mutations into PH c(552) at five s...
متن کاملQuaternary structure of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa and its reoxidation with a novel cytochrome c from this organism.
Quinoprotein (2,7,9-tricarboxy-1H-pyrrolo-[2,3-f]quinoline-4,5-dione quinone form (PQQ)-containing) ethanol dehydrogenase (EDH) from Pseudomonas aeruginosa ATCC 17933 was purified to homogeneity. EDH has an alpha 2 beta 2 configuration and subunits comparable in size to those of methanol dehydrogenase (MDH). Compared with other PQQ-containing dehydrogenases, Ca2+ is rather loosely bound and it ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Biochemical journal
دوره 89 شماره
صفحات -
تاریخ انتشار 1963