T. Nikai et al., CHARACTERIZATION AND AMINO-TERMINAL SEQUENCE OF PHOSPHOLIPASE A(2)-IIFROM THE VENOM OF AGKISTRODON BILINEATUS (COMMON CANTIL), International Journal of Biochemistry, 26(1), 1994, pp. 43-48
1. Phospholipase A(2) was isolated from the venom of Agkistrodon bilin
eatus by Sephadex G-75 and CM-Cellulose column chromatographies. 2. Th
e purified phospholipase A(2) gave a single band on disc polyacrylamid
e gel electrophoresis, sodium dodecyl sulfate polyacrylamide gel elect
rophoresis and ODS-HPLC. 3. The enzyme preparation had a mel. wt of 14
,000, isoelectric point of pH 10.12 and possessed 121 amino acid resid
ues. 4. The enzyme hydrolyzed the phospholipids phosphatidyl choline,
phosphatidyl ethanolamine, phosphatidyl inositol and phosphatidyl seri
ne. 5. The contraction of mouse diaphragm was inhibited by phospholipa
se A(2)-II. 6. Phospholipase A(2) activity of this preparation was inh
ibited by ethylenediamine tetraacetic acid, ethlyleneglycol (beta-amin
oethyl) N,N,N',N'-tetraacetic acid, p-bromophenacyl bromide or N-bromo
succinimide, but not by iodoacetic acid or diisopropyl fluorophosphate
. 7. The amino-terminal sequence of the PLA(2)-II was determined.