Structure<unk>  was successfully isolated from O. Hannah venom by gel filtration and cation-exchange chromatography. Its molecular weight is 25 kDa (from positions 19 – 239), which conforms to the molecular mass predicted from its cDNA sequences. Homology<unk>  is a cysteine-rich secretory protein and therefore belongs to the CRISP family. These proteins possess 16 strictly conserved cysteines and contain 8 disulfide bonds. Ten of the 16 cysteine residues are clustered at the C-terminal end of the protein.<unk>  belongs to the “long” CRISPs subgroup, which consists of the 9 CRISPs with the longest sequences. Snake venom CRISPs belonging to different subgroups act on different biological targets, contributing in this way to the diversity of damaging effects of snake venoms. Family The phylogenetic tree constructed from the nucleotide sequences of all known snake venom CRISPs shows that<unk>  is more closely related to the Viperidae branch than the Elapidae branch even though O. Hannah belongs to the Elapidae snakes.<unk> , along with other specific snake toxins like triflin and ablomin, is also a helothermine-related venom protein (Helveprin) which was originally isolated from the skin of the Mexican beaded lizard.
Ophanin
Melanin
Cellulite
Ceruloplasmin
Hematoporphyrin
Respiratory pigment
Canthaxanthin
Kerion