Accession Number:

AD0728504

Title:

Isolation of Snake Venom Toxins and Study of Their Mechanism of Action

Descriptive Note:

Final technical rept.

Corporate Author:

ROGOFF-WELLCOME MEDICAL RESEARCH INST PETAH TIQWA (ISRAEL)

Personal Author(s):

Report Date:

1971-01-01

Pagination or Media Count:

54.0

Abstract:

A hemorrhagin from Echis coloratus venom, which appeared as a single protein in immunoelectrophoresis and in disc electrophoresis, possessed both hemorrhagic and proteolytic activities. Some of its antigenic determinants were identical to those of Vipera palestinae hemorrhagin. Partial cross neutralization of the lethal activity of V.p. hemorrhagin and of E.c. venom by heterologous antiserum was obtained. Phospholipases A from the venoms of Naja naja and V.p. are able to hydrolyze lysolecithin at alkaline pH. Haemachatus haemachatus Ringhals cobra phospholipase A hydrolyzes phospholipids of brain cell membranes and destroys part of the membranal system for histidine uptake. A direct lytic factor from Ringhals venom, known to interact with unmodified red cell membranes, acts equally well on sialic-acid-depleted membranes. E.c. venom administered intravenously causes damage to mouse brain capillary endothelial cells revealed by electron microscopy.

Subject Categories:

  • Toxicology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE