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PMID:10965034
| Citation |
Koyanagi, S, Nagata, K, Tamura, T, Tsukita, S and Sone, N (2000) Purification and characterization of cytochrome c-553 from Helicobacter pylori. J. Biochem. 128:371-5 |
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| Abstract |
Helicobacter pylori, a microaerophilic Gram-negative spiral bacterium residing in the human stomach, contains a small size soluble cytochrome c. This cytochrome c was purified from the soluble fraction of H. pylori by conventional chromatographies involving octyl-cellulose and CM-Toyopearl. Its reduced form gave an alpha absorption band at 553 nm, and thus the cytochrome was named H. pylori cytochrome c-553. The cytochrome, giving a band below 10,000 Da upon SDS-PAGE, was determined to have a mass of 8,998 by time of flight mass spectroscopy. Its N-terminal peptide sequence was TDVKALAKS---, indicating that the nascent polypeptide was cleaved to produce a signal peptide of 19 amino acid residues and a mature protein composed of 77 amino acid residues. The cb-type cytochrome c oxidase oxidized ferrocytochrome c-553 of this bacterium actively (V(max) of about 250 s(-1)) with a small K(m) (0.9 microM). Analysis of the effect of the salt concentration on the oxidase activity indicated that oxidation of cytochrome c-553 is highly inhibited under high ionic conditions. The amino acid sequence of H. pylori cytochrome c-553 showed the closest similarity to that of Desulfovibrio vulgaris cytochrome c-553, and these sequences showed a weak relationship to that of the cytochrome c(8)-group among class I cytochromes c. |
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| Keywords |
Amino Acid Sequence; Chromatography, Ion Exchange; Cytochrome c Group/chemistry; Cytochrome c Group/isolation & purification; Electrophoresis, Polyacrylamide Gel; Helicobacter pylori/enzymology; Hydrogen-Ion Concentration; Mass Spectrometry; Molecular Sequence Data; Molecular Weight; Oxidation-Reduction; Potassium Chloride/metabolism; Sequence Homology, Amino Acid |
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