Abstract:
:A novel serum protein inhibiting specifically the enzymatic activity of the basic phospholipase A(2) (PLA(2)) from the venom of the Chinese mamushi snake (Agkistrodon blomhoffii siniticus) was purified from a nonvenomous Colubridae snake, Elaphe quadrivirgata. The purified inhibitor was a 150-kDa glycoprotein having a trimeric structure, composed of two homologous 50-kDa subunits. Their amino acid sequences, containing leucine-rich repeats, were typical of the beta-type PLA(2) inhibitor (PLIbeta), previously identified from the serum of A. blomhoffii siniticus. The inhibitor inhibited exclusively group II basic PLA(2)s and did not inhibit other kinds of PLA(2)s. This is the first paper reporting the existence of PLIbeta in a nonvenomous snake. The existence of PLIbeta in the nonvenomous snake reflects that PLIbetas are widely distributed over the snake species and participate commonly in regulating the physiological activities of the unidentified target PLA(2)s.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Okumura K,Inoue S,Ikeda K,Hayashi Kdoi
10.1016/s0003-9861(02)00551-9subject
Has Abstractpub_date
2002-12-01 00:00:00pages
124-30issue
1eissn
0003-9861issn
1096-0384pii
S0003986102005519journal_volume
408pub_type
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