期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 408, 期 1, 页码 124-130出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0003-9861(02)00551-9
关键词
phospholipase A(2); phospholipase A(2) inhibitor; snake serum; leucine-rich repeats; amino acid sequence; cDNA cloning
A novel serum protein inhibiting specifically the enzymatic activity of the basic phospholipase A (PLAN) 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 PLA2 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. (C) 2002 Elsevier Science (USA). All rights reserved.
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