| Literature DB >> 1122291 |
Abstract
Reduced and S-carboxymethylated phospholipase A (Fraction DE-III) from Naja melanoleuca venom was digested with trypsin, chymotrypsin and thermolysin. The resulting peptides were purified by ion-exchange chromatography on DEAE-cellulose, gel filtration on Sephadex G-25 or G-50 and chromatography and electrophoresis on paper. The amino acid sequences of the intact enzyme and the pur peptides were determined by the Edman procedure, either through the use of the automatic sequencer or by manual manipulation. The chymotryptic digest provided the necessary overlapping peptides which allowed the alignment of the tryptic peptides into a single chain of 119 amino acids. The amino acid sequence of N. melanoleuca phospholipase A shows a high degree of homology with phospholipases A from Bitis gabonica and also from porcine pancreas.Entities:
Mesh:
Substances:
Year: 1975 PMID: 1122291
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002