title: 'Partitagin', a unique β, γ-fibrinogenase that inhibits platelet aggregation from Hippasa partita spider venom.
abstract: Partitagin, a Zn-containing hemorrhagic metalloprotease from Hippasa partita spider venom gland extract has been purified and studied for its dermonecrotic and myonecrotic effects. In the present study, Partitagin has been studied for its effect on fibrinogen, fibrin and platelet aggregation. Partitagin incubated with fibrinogen preferentially cleaved Bβ chain and later γ-chain upon prolonged incubation period (16 h). Partitagin upon incubation with fibrin degraded γ-dimer chain. Partitagin inhibited collagen-triggered platelet aggregation. The proteolytic activity of Partitagin was inhibited by serum α2-macroglobulin (α2-M). This is the first report describing β, γ-fibrinogenase having inhibitory effect on platelet aggregation.
authors.affiliation: Department of Medicine, Division of Immunology and Rheumatology, Stanford University, Stanford, CA, USA. nagarajubiochem@gmail.com
authors.forename: Nagaraju
authors.initials: N
authors.lastname: Shivaiah
authors.forename: Kemparaju
authors.initials: K
authors.lastname: Kempaiah
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005337:Fibrin / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism; D006801:Humans; D045726:Metalloproteases / Q000302:isolation & purification* / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010974:Platelet Aggregation / Q000187:drug effects*; D013111:Spider Venoms / Q000201:enzymology*; D013112:Spiders / Q000201:enzymology*
chemical_list: D013111:Spider Venoms; D005337:Fibrin; D005340:Fibrinogen; D045726:Metalloproteases