Covalent structural analysis of yeast inorganic pyrophosphatase

The present paper describes the amino acid sequence analysis of the internal and COOH-terminal cyanogen bromide fragments of yeast inorganic pyrophosphatase (Sterner, R., Noyes, C., and Heinrikson, R.L. (1974) Biochemistry 13, 91-99). This information coupled with that derived from earlier structura...

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Bibliographic Details
Published in:The Journal of biological chemistry 1978-02, Vol.253 (3), p.889-897
Main Authors: Cohen, S A, Sterner, R, Keim, P S, Heinrikson, R L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Peptide Fragments
Pyrophosphatases
Saccharomyces cerevisiae - enzymology
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Summary:The present paper describes the amino acid sequence analysis of the internal and COOH-terminal cyanogen bromide fragments of yeast inorganic pyrophosphatase (Sterner, R., Noyes, C., and Heinrikson, R.L. (1974) Biochemistry 13, 91-99). This information coupled with that derived from earlier structural studies of the enzyme (Sterner, R., AND Heinrikson, R.L. (1975) Arch. Biochem. Biophys. 165, 693-703) provides the complete covalent structure of the pyrophosphatase subunit. The majority of the sequence data was derived from automated Edman degradation of the intact cyanogen bromide fragments and the large tryptic peptides obtained from citraconylated derivates in which cleavages were restricted to arginyl residues. The structural determination was completed by analysis of tryptic and chymotryptic peptides from the decitraconylated fragments. The monomer peptide chain contains 285 amino acid residues and the molecular weight calculated from the sequence analysis is 32,042.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)38188-7