Abstract:
:Two hemorrhagic proteases, Lachesis hemorrhagic toxins a and b (LHTa and LHTb), were isolated from the venom of Lachesis muta, which is distributed in Central and South America. One protease showed strong hemorrhagic action, while the other showed weak hemorrhagic activity even though the two enzymes are very similar in their chemical properties. Neither enzyme hydrolyzed arginine esters, but both hydrolyzed casein and reduced fibrinogen. The A alpha chain of fibrinogen was hydrolyzed first, and the B beta chain was hydrolyzed later. The gamma chain of fibrinogen was resistant to hydrolysis. The molecular weights of LHTa and LHTb were very similar, 22,000 and 23,000, respectively. The amino acid composition of LHTa was also similar to that of LHTb. The secondary structure of LHTa as determined by Lippert's equation was 52% alpha helix, 17% beta sheet, and 31% random coil; that of LHTb was 47% alpha helix, 13% beta sheet, and 40% random coil.
journal_name
Chem Res Toxicoljournal_title
Chemical research in toxicologyauthors
Ran YL,Zheng SD,Tu ATdoi
10.1021/tx00006a003subject
Has Abstractpub_date
1988-11-01 00:00:00pages
337-42issue
6eissn
0893-228Xissn
1520-5010journal_volume
1pub_type
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