Isolation and characterization of biological properties of inhibitors angiotensin-1-converting enzyme from the spider venom Latrodectus tredecimguttatus.
For the first time by method of gel-filtration and ionexchange chromatography two bradykinin-potentiating peptides have been isolated in homogeneous state from Latrodectus tredecimguttatus spider venom. The homogeneity was proved by disk-electrophoresis, isoelectrical focusing, analysis of aminoacid content and rechromatography. Peptides are acid proteins with molecular mass 10,000 and 2500 D. Peptides prolong depressor effects of bradykinin, stimulate histamine releasing from cells, decrease blood pressure in rats.
Akchunov
A A
AA
Institute of Bioorganic Chemistry, Tashkent, Uzbekistan.
Golubenko
Z
Z
Sosnina
N
N
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D000818:Animals; D001794:Blood Pressure / Q000187:drug effects; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D066298:In Vitro Techniques; D007668:Kidney / Q000187:drug effects / Q000201:enzymology; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D051381:Rats; D013111:Spider Venoms / Q000737:chemistry*
D000806:Angiotensin-Converting Enzyme Inhibitors; D009842:Oligopeptides; D013111:Spider Venoms; C006791:bradykinin potentiating factors; D007703:Peptidyl-Dipeptidase A