Magalhaes A, Da Fonseca B C, Diniz C R, Gilroy J, Richardson M
Centro de Pesquisa e Desenvolvimento, Fundacão Ezequiel Dias, Belo Horizonte (MG), Brazil.
FEBS Lett. 1993 Aug 23;329(1-2):116-20. doi: 10.1016/0014-5793(93)80205-9.
The complete amino acid sequence of a thrombin-like enzyme with gyroxin activity isolated from the venom of the bushmaster snake Lachesis muta muta was determined by automated and DABITC/PITC microsequencing of the intact protein; fragments derived from it by separate cleavages with cyanogen bromide, iodosobenzoic acid and hydroxylamine; and peptides resulting from enzymatic digestions with trypsin, pepsin, chymotrypsin, and elastase. The protein, which is composed of 228 residues, contains four putative sites of N-linked glycosylation and exhibits significant sequence similarities with other serine proteases reported from snake venoms.