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Biomedical subjects

A T Tu

Publications and source records attributed to A T Tu.

151 records · Page 9Linked to original sources
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Effect of diethylenetriaminepentaacetic acid and procaine on hemorrhage induced by rattlesnake venom.

Nineteen compounds and seven combinations of compounds were tested for their ability to neutralize the hemorrhagic activity of Crotalus atrox venom in vitro and in vivo. Two compounds and four combinations were effective in reducing hemorrhage in an in vivo test in which the venom was injected before injection of compounds. DTPA plus procaine HCl was the most effective combination and reduced hemorrhage when injected 1, 5, or 15 minutes after injection of venom. DTPA-procaine reduced hemorrhage induced by injection of C. atrox venom into dogs as well as mice. DTPA in combination with procaine did not reduce myonecrosis or lethality resulting from injection of venom into mice, but it could be used in conjunction with antivenin to treat local tissue damage resulting from rattlesnake venom poisoning.

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Raman studies on bradykinin and a cyclic bradykinin.

Laser Raman spectra of bradykinin in water, deuterium oxide, and the solid phase were recorded. From the spectra it was concluded that bradykinin conformation is comprised of ordered and unordered structure. The ordered structure appears to be some form of reverse turn. Furthermore, it seems that there is an enhancement of the turn structure in the solid phase. A cyclic cystine containing analog of bradykinin was also examined with Raman spectroscopy. The cyclic bradykinin analog gives a Raman spectrum very similar to that of the linear bradykinin and therefore must share similar conformational forms with bradykinin. The restrictive Cys-Cys disulfide in the cyclic bradykinin must serve to maintain a conformation acceptable to bradykinin receptors since the cyclic peptide exhibits biological activity.

Bradykinin↗
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Sea snake bites.

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Animals↗
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Biochemical characterization of two hemorrhagic proteases from the venom of Lachesis muta (bushmaster).

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.

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