| Literature DB >> 179530 |
Abstract
The molecular weight and amino acid composition of phosphoglycerate mutase from yeast were determined. CNBr cleavage produced a large (190-residue) fragment and a small (60-residue) fragment. Tryptic and chymotryptic peptides derived from the large fragment were fractionated by ion-exchange chromatography. Peptides from two histidine-containing regions were isolated and the amino acid sequences were determined. Correlation of these data with X-ray-crystallographic evidence shows that the histidine residue in the sequence Arg-Leu Asn-Glu-Arg-His-Tyr-Gly-Asp-Leu-Glu-Gly-Lys is located at the active site.Entities:
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Year: 1976 PMID: 179530 PMCID: PMC1172556 DOI: 10.1042/bj1530145
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857