Purification and properties of an anionic zymogen of phospholipase a from porcine pancreas
作者： G.H. De Haas , N.M. Postema , W. Nieuwenhuizen , L.L.M. Van Deenen
DOI: 10.1016/0005-2744(68)90249-0
关键词: Residue (chemistry) 、 Trypsin 、 Glutamic acid 、 Phospholipase A 、 Amino acid 、 Zymogen 、 Chemistry 、 Biochemistry 、 Peptide sequence 、 Phospholipase B
摘要: Abstract 1. This paper describes the isolation and purification of an enzymically inactive precursor porcine pancreatic phospholipase A (phosphatide acyl-hydrolase, EC 3.1.1.4). 2. The protein, which has a molecular weight about 15 000, appears to consist single polypeptide chain, terminating at NH 2 region in amino acid sequence: Glu-Gly-Glu-Ile-Ser-Ser-Arg-Ala......, having cystine as COOH-terminal acid. 3. molecule is activated by trypsin splits above -Arg-Ala-peptide bond, yielding active heptapeptide: Glu-Gly-Glu-Ile-Ser-Ser-Arg. 4. In this released peptide, well itself, N-terminal glutamic residue no free α-NH group. 5. Phospholipase A, isolated from autolysed tissue, be identical with product obtained activation pure precursor.
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