Amino Acid Composition and NH2-Terminal Amino Acid Sequence of Rat Platelet Secretory Phospholipase A21
- 1 May 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 101 (5), 1311-1314
- https://doi.org/10.1093/oxfordjournals.jbchem.a121996
Abstract
The amino acid composition and partial NH 2 -terminal amino acid sequence of the phospholipase A 2 secreted by stimulated rat platelets were determined. The most predominant amino acid in the phospholipase A 2 was cysteine followed by lysine, suggesting that it is a basic one. This finding is consistent with its high affinity to a cation exchange column. The NH 2 -terminal 24 amino acids were found to be as follows: X-Leu-Leu-Glu-Phe-Gly-Met-IIe-Leu-phe-Lys-Thr-Gly-Lys-Arg-Ala-Asp-Val-Ser-Tyr-Gly-Phe-Tyr-Gly- The enzyme contains 5 Phe, 8 Met, 9 lle, 24 Tyr, and 25 Gly residues, all of which are conserved in the sequenced pancreatic phospholipase A 2 .This is the first report of the tentative characterization of a cukaryotic phospholipase A 2 , the cellular source of which is known,i.e., it does not originate from a venom or the pancreas.This publication has 3 references indexed in Scilit:
- Dog and Rat Pancreatic Phospholipases A2: Complete Amino Acid Sequences Deduced from Complementary DNAsThe Journal of Biochemistry, 1986
- Characterization of phospholipase a from pulmonary secretions of patients with alveolar proteinosisBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1977
- The primary structure of phospholipase A2 from porcine pancreas A reinvestigationBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977