Literature DB >> 1191259

The amino acid sequence of cytochrome f from the brown alga Alaria esculenta (L.) Grev.

M V Laycock.   

Abstract

Cytochrome f was isolated from the brown alga Alaria esculenta and the amino acid sequence was determined. The native haemoprotein has a molecular weight of 9800 and consists of a single polypeptide chain of 86 amino acid residues with a haem group bonded to cysteine residues at positions 14 and 17. The N-terminus is not acetylated and no methylated lysines were found. Sequences of three other algal cytochromes f were compared with that of Alaria and 22 out of 92 positions were common to the four sequences. One-half of these conserved sites occur between positions 49 and 63. Detailed evidence for the amino acid sequence of Alaria cytochrome has been deposited as Supplementary Publication SUP 50048 (6 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975) 145, 5.

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Year:  1975        PMID: 1191259      PMCID: PMC1165613          DOI: 10.1042/bj1490271

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  15 in total

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5.  The amino acid sequence of cytochrome c-553 from the Chrysophycean alga Monochrysis lutheri.

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6.  Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi.

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Journal:  Proc Natl Acad Sci U S A       Date:  1965-12       Impact factor: 11.205

Review 7.  Strategy and tactics in protein chemistry.

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8.  Molecular weight determination from amino acid analysis data: a numerical method.

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9.  Purification and characterization of cytochrome 553 from the chrysophycean alga Monochrysis lutheri.

Authors:  M V Laycock; J S Craigie
Journal:  Can J Biochem       Date:  1971-06

10.  Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups.

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  1 in total

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