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The primary structure of bovine pancreatic phospholipase A2.
The complete amino acid sequence of bovine phospholipase A2 (EC 3.1.1.4) was determined. This enzyme has a molecular weight of 13 782 and consists of a single polypeptide chain of 123 amino acids cross-linked by seven disulfide bridges. The main fragmentation of the polypeptide chain was accomplished by digesting the reduced and thialaminated derivative of the protein with trypsin, staphylococcal protease and cyanogen bromide. A number of chymotryptic peptides were used for alignment and to obtain overlaps of at least two residues. The sequence of the peptides was determined by Edman degradation by means of direct phenylthiohydantoin identification in combination with identification as dansyl amino acids. Although 71% of all residues of phospholipase A2 from bovine, porcine and equine sources are conserved, bovine phospholipase A2 differs from the others by the total number of residues and by substitutions at 20 (porcine) and 33 (equine) positions.
PMID: 620674 [PubMed - indexed for MEDLINE]
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Cited by 4 PubMed Central articles
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Amino acid sequences of three phospholipases A I, III and IV from the venom of the sea snake Laticauda semifasciata.
Nishida S, Kim HS, Tamiya N.
Biochem J. 1982 Dec 1; 207(3):589-94.
[Biochem J. 1982]
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Sequence of a cDNA coding for bovine pancreatic phospholipase A2.
Tanaka T, Kimura S, Ota Y.
Nucleic Acids Res. 1987 Apr 10; 15(7):3178.
[Nucleic Acids Res. 1987]
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Isolation, properties and amino acid sequences of a phospholipase A2 and its homologue without activity from the venom of a sea snake, Laticauda colubrina, from the Solomon Islands.
Takasaki C, Kimura S, Kokubun Y, Tamiya N.
Biochem J. 1988 Aug 1; 253(3):869-75.
[Biochem J. 1988]
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