The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. I. Tryptic peptides

A total of 25 tryptic peptides was isolated from the S-beta-carboxymethyl derivative of Clostridium pasteurianum iron protein (N2). In order to obtain the various peptides in pure state, a combination of gel permeation, cation and anion exchange column chromatographic methods, as well as various asc...

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Bibliographic Details
Published in:The Journal of biological chemistry 1977-10, Vol.252 (20), p.7081-7088
Main Authors: Tanaka, M, Haniu, M, Yasunobu, K T
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Clostridium - enzymology
Ferredoxins
Nitrogenase
Peptide Fragments - analysis
Trypsin
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Summary:A total of 25 tryptic peptides was isolated from the S-beta-carboxymethyl derivative of Clostridium pasteurianum iron protein (N2). In order to obtain the various peptides in pure state, a combination of gel permeation, cation and anion exchange column chromatographic methods, as well as various ascending paper chromatographic methods were adopted. Sequence studies of the tryptic peptides were carried out mainly by a modified manual Edman degradation procedure and also by automated analysis, carboxypeptidase digestion, and by hydrazinolysis. Thus, 242 residues (88.6%) out of a total of 273 amino acid residues were sequenced in the present study. The sum of the amino acid residues in the tryptic peptides isolated from iron protein (N2) accounted for the 273 amino acid residues present in the iron protein.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)66937-1