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Accelerated evolution of crotalinae snake venom gland serine proteases
Author(s) -
Deshimaru Masanobu,
Ogawa Tomohisa,
Nakashima Kin-ichi,
Nobuhisa Ikuo,
Chijiwa Takahito,
Shimohigashi Yasuyuki,
Fukumaki Yasuyuki,
Niwa Mineo,
Yamashina Ikuo,
Hattori Shosaku,
Ohno Motonori
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01144-1
Subject(s) - proteases , venom , biology , serine , isozyme , complementary dna , serine protease , gene , biochemistry , microbiology and biotechnology , protease , enzyme
Eight cDNAs encoding serine proteases isolated from Trimeresurus flavoviridis (habu snake) and T. gramineus (green habu snake) venom gland cDNA libraries showed that nonsynonymous nucleotide substitutions have accumulated in the mature protein‐coding regions to cause amino acid changes. Southern blot analysis of T. flavoviridis genomic DNAs using two proper probes indicated that venom gland serine protease genes form a multigene family in the genome. These observations suggest that venom gland serine proteases have diversified their amino acid sequences in an accelerating manner. Since a similar feature has been previously discovered in crotalinae snake venom gland phospholipase A 2 (PLA 2 ) isozyme genes, accelerated evolution appears to be universal in plural isozyme families of crotalinae snake venom gland.