Ophanin, piscivorin, ablomin, latisemin and triflin, cysteine-rich secretory proteins that can reduce muscle contractions, are naturally found where?
Latisemin of some other snake venom toxins from the CRISP family, like ablomin from the Japanese Mamushi snake and triflin from the Habu snake. They also inhibit cyclic nucleotide-gated ion channels. Other snake venom proteins in the CRISP family: Latisemin Latisemin is a cysteine-rich secretory protein that can be isolated from the venom of the Black-banded sea krait, a sea snake indigenous to the warmer waters of the western Pacific Ocean. It is a toxin that inhibits cyclic nucleotide-gated ion channels and blocks L-type calcium channels, thereby reducing smooth muscle contraction. Latisemin is a component of the venom produced by the
Cysteine-rich secretory protein the oocyte-sperm binding needed for fertilisation. Given the involvement of CRISPs in several stages of human reproduction, it is unsurprising that applications in treatment of infertility and as contraceptives are being actively investigated. CRISPs are found in the venom of a wide variety of snake species. Examples include ablomin from the Japanese Mamushi snake ("Gloydius blomhoffi", formerly "Agkistrodon blomhoffi"), latisemin from the Erabu sea snake ("Laticauda semifasciata"), ophanin from the King Cobra ("Ophiophagus hannah"), piscivorin from the Eastern Cottonmouth ("Agkistrodon piscivorus") and triflin from the Habu snake ("Trimeresurus flavoviridis") – each of these proteins is named for the snake species