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Purification and characterization of cytochrome c-553 from Helicobacter pylori.

Purification and characterization of cytochrome c-553 from Helicobacter pylori. Research Abstract Details 

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  • Purification and characterization of cytochrome c-553 from Helicobacter pylori. Abstract Text:

    s koyanagiS Koyanagi,k nagataK Nagata,t tamuraT Tamura,s tsukitaS Tsukita,n soneN Sone,

    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.

    Purification and characterization of cytochrome c-553 from Helicobacter pylori. Publishing Authors By Initials

    s koyanagiS Koyanagi,k nagataK Nagata,t tamuraT Tamura,s tsukitaS Tsukita,n soneN Sone,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research

    PUBMED ID PMID:

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    Purification and characterization of cytochrome c-553 from Helicobacter pylori. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 128

    Page Numbers: 371-5

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Sep

    YEAR: 2000

    Purification and characterization of cytochrome c-553 from Helicobacter pylori. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Purification and characterization of cytochrome c-553 from Helicobacter pylori. Keywords Mesh Terms:

    KEYWORDS: Sequence Homology, Amino Acid

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Purification and characterization of cytochrome c-553 from Helicobacter pylori. Information

    Substance Name: cytochrome C-552

    Registry Number: 9048-78-6

    Grant and Affiliation Information for Purification and characterization of cytochrome c-553 from Helicobacter pylori.

    AFFILIATION: Department of Biochemical System Engineering, Kyushu Institute of Technology, Kawazu Iizuka, Fukuoka 820-8502, Japan. sone@bse.kyutech.ac.jp

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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