Characterization of mocarhagin, a cobra venom metalloproteinase from Naja mocambique mocambique, and related proteins from other Elapidae venoms.
Mocarhagin, a cobra venom metalloproteinase from Naja mocambique mocambique, has previously been shown to cleave selectively two mucin-like substrates on platelets and neutrophils within anionic amino acid sequences containing sulfated tyrosines. We now show that purified mocarhagin has haemagglutinin activity, and a similar profile for inhibition of mocarhagin-dependent haemagglutination and proteolysis suggests that the lectin-like domain may account for its substrate specificity. In addition, immunologically and functionally related proteins were detected in other Elapidae venoms.
Ward
C M
CM
Hazel and Pip Appel Vascular Biology Laboratory, Baker Medical Research Institute, Prahran, Victoria, Australia.
Vinogradov
D V
DV
Andrews
R K
RK
Berndt
M C
MC
D000818:Animals; D004546:Elapid Venoms / Q000201:enzymology*; D006384:Hemagglutination / Q000187:drug effects; D008666:Metalloendopeptidases / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology*; D019038:Platelet Glycoprotein GPIb-IX Complex / Q000378:metabolism
D004546:Elapid Venoms; D019038:Platelet Glycoprotein GPIb-IX Complex; C023592:glycocalicin; D008666:Metalloendopeptidases; C099092:mocarhagin