Purification and amino acid sequence of basic protein I, a lysine-49-phospholipase A2 with low activity, from the venom of Trimeresurus flavoviridis (Habu snake)

Structural Characteristics and Evolution of theProtobothrops elegansPancreatic Phospholipase A2Gene in Contrast with Those ofProtobothropsGenus Venom Phospholipase A2Genes

“…6,7) Group III PLA 2 s are found in bee venoms 8) and ubiquitous tissues. 9 14,17,18) This accords with their branching patterns, in the phylogenetic tree. 19) Mathematical examination of the nucleotide sequences of their cDNAs and genes has revealed that they evolved via Darwinian-type accelerated evolution, acquiring diverse physiological activities.…”

“…Then, in order to obtain an entire fragment harboring the P. elegans pancreatic PLA 2 gene and its 5 0 and 3 0 flanking regions, inverted PCRs were conducted against the liver genomic DNAs following the manufacturer's protocol (Toyobo, Osaka) starting from this 486-nt segment with restriction enzymes, Bal I, Bcl I, EcoR I, Nsi I, Pvu II, Sac I, Sph I, and Ssp I (Nippon Gene, Osaka). The primers employed in PCR against internally ligated fragments were PPP1, 5,6,7,10,11,12,16,17,18,19, and 22, which were based on the known sequences of the previously obtained PCR fragments. The position numbers and sequences of the primers are given in Table 1 0 -CAGCTGCTCCGGAGA-GGAATTGTGAN-3 0 , which can anneal to the 3 0 terminal portion of the 3 0 flanking region of the pancreatic PLA 2 gene, were prepared.…”

Structure of a calcium-independent phospholipase-like myotoxic protein fromBothrops aspervenom

“…Recently, a sub-class of snake-venom PLA2-1ike proteins which retain cytotoxicity, but lack phospholipase activity have been identified and sequenced (Maraganore et al, 1984;Maraganore, Poorman & Heinrickson, 1987;Yoshizumi et al, 1990;Liu et al, 1990;Homsi-Brandenburgo, Queiroz, Santo-Neto, Rodrigues-Simon & Giglio, 1988;Francis, Gutierrez, Lomonte & Kaiser, 1991). In the catalytically active PLA2, calcium is an essential co-factor, and the noncatalytic PLA2-1ike proteins are primarily characterized by the substitution of Asp49 by Lys.…”

Accelerated Evolution of Fetuin Family Proteins inProtobothrops flavoviridis(Habu Snake) Serum and the Discovery of an L1-Like Genomic Element in the Intronic Sequence of a Fetuin-Encoding Gene

“…For example, among PLA 2 isozymes of P. flavoviridis (the habu snake), the Asp49 PLA 2 shows phospholipase activity, whereas basic proteins I and II, with potent myotoxicities, show only very weak enzymatic activity. 1,[4][5][6][7] Furthermore, the physiological activities of the enzymes of the MP family of snake venom vary considerably: some induce hypodermic hemorrhage and others trigger apoptotic cell death. 3) Comparisons of the nucleotide sequences of the genes for such snake venom isozymes have revealed a striking feature, that nucleotide substitutions have occurred substantially more in the protein-coding sequences than in the noncoding sequences.…”