The primary structure of rat platelet phospholipase A2.
In our previous report (Hayakawa, M., Kudo, I., Tomita, M., & Inoue, K. (1988) J. Biochem. 103, 263-266), we have shown that phospholipases A2 purified from rat platelet membrane fractions and an extracellular medium of thrombin-stimulated rat platelets were essentially identical to each other. Both purified enzymes were digested with proteases, and the resulting peptides were subjected to primary sequence determination. The sequence analysis of the HPLC-separated peptides and the alignment of the sequences showed a tentative primary structure of rat platelet phospholipase A2, which was composed of 125 amino acid residues. It showed 47% homology with snake venom Agkistrodon halys blomhoffii phospholipase A2.
Hayakawa
M
M
Department of Health Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo.
Kudo
I
I
Tomita
M
M
Nojima
S
S
Inoue
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001792:Blood Platelets / Q000201:enzymology; D002462:Cell Membrane / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010740:Phospholipases / Q000097:blood*; D010741:Phospholipases A / Q000097:blood*; D054467:Phospholipases A2; D051381:Rats; D012697:Serine Endopeptidases
D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; C036813:lysyl endopeptidase