Prokaryote-eukaryote relationship and the amino acid sequence of plastocyanin from Anabaena variabilis
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چکیده
منابع مشابه
The Amino Acid Sequence of Chlorella fusca Plastocyanin
The sequences proposed in Fig. 1 for the Ps. aerirgirioJa and Ps. strrtzeri proteins have been confirmed by the isolation and characterization of the expected peptides from tryptic digests of the haeni-free proteins. From each of these two proteins a second tryptic peptide was isolated that contained two residues of cysteine and a residue of histidine. The amino acid composition was such that t...
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The resident microbiota of the human gastrointestinal (GI) tract is comprised of ~2000 bacterial species, the majority of which are anaerobes. Colonization of the GI tract is important for normal development of the immune system and provides a reservoir of catabolic enzymes that degrade ingested plant polysaccharides. Bacteroides fragilis is an important member of the microbiota because it cont...
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Plastocyanins are low-molecular-weight cuproproteins, which occur in the chloroplasts of plants and algae. The exact biological function of the protein remains uncertain, but is probably associated with photosynthetic electron transport (Gregory, 1971). The small size and blue colour of the protein simplify the purification of plastocyanin, and studies with a number of species have been reporte...
متن کاملThe amino acid sequence of plastocyanin from Vicia faba L. (broad bean).
The amino acid sequence of plastocyanin from broad bean was determined. It consists of a single polypeptide chain of 99 residues. The sequence was determined by using a Beckman 890C sequencer and by dansyl-phenyl isothiocyanate analysis of peptides obtained by the enzymic cleavage of purified cyanogen bromide fragments. Some parts of the sequence depend on the results of Edman degradation of pe...
متن کاملThe amino acid sequence of plastocyanin from French bean (Phaseolus vulgaris).
The amino acid sequence of the plastocyanin from French bean (Phaseolus vulgaris) was determined. The protein consists of a single polypeptide chain of 99 residues, and the sequence was determined by characterization of CNBr, tryptic, chymotryptic and thermolysin peptides. When the sequence is compared with that from the plastocyanin of the unicellular green alga Chlorella fusca, the French-bea...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1975
ISSN: 0264-6021
DOI: 10.1042/bj1490675