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Abstract
The amino acid sequence of a thrombin like enzyme, named elegaxobin, isolated from
the venom of Trimeresurus elegans (Sakishima-habu) was determined by Edman sequencing
of the peptides, derived from digests with cyanogen bromide, hydroxylamine, achromobacter
protease I, trypsin, V8 protease, and chymotrypsin. Elegaxobin showed conservation
of the catalytic amino acid residues (His, Asp, and Ser) of trypsin like serine protease
in the amino acid sequence. The carboxy-terminal amino acid, Leu, was determined using
carboxypeptidase Y. Elegaxobin consisted of 233 amino acids and had a calculated molecular
weight of 25,439. Elegaxobin was 53, 59, 26 and 40% homologous in sequence to ancrod,
flavoxobin, bovine thrombin and trypsin, respectively.