1981
DOI: 10.1055/s-0038-1650177
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Studies on the Degradation of Fibrinogen by Proteolytic Enzymes from the Larvae of Lanomia achelous (Cramer)

Abstract: SummaryFibrinogen degradation products formed by the action of purified haemolymph and saliva of a Satumidae caterpillar of the Lonomia genus were studies by immunoelectrophoresis and polyacrylamide/SDS gel electrophoresis.The pattern of degradation differ form the one described for plasmin, trypsin, brinase and ochrase. The most striking difference being the rapid loss of the a chain in spite of the presence of the protease inhibitor aprotinin, and/or denaturalizing agents such as 8 M Urea and 2% SDS.

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Cited by 22 publications
(7 citation statements)
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“…Considering the high levels of FDP's it was surprising to observe no inhibitory effect (total correction with normal plasma). "In vitro" we have been able to demonstrate that the human fibrinogen split fragments behave electrophoretically and immunologically very differently in comparison to those obtained through the "classical" plasmin degradation (26). Presumably, "in vivo" the venom's enzymes are capable of inducing a heterogeneous group of FDP's: some originate from the typical fibrinolytic pathway, while others evolve when enzymatic activities are targeted on different sites of the fibrinoger/fibrin molecules.…”
Section: Case Reportsmentioning
confidence: 95%
“…Considering the high levels of FDP's it was surprising to observe no inhibitory effect (total correction with normal plasma). "In vitro" we have been able to demonstrate that the human fibrinogen split fragments behave electrophoretically and immunologically very differently in comparison to those obtained through the "classical" plasmin degradation (26). Presumably, "in vivo" the venom's enzymes are capable of inducing a heterogeneous group of FDP's: some originate from the typical fibrinolytic pathway, while others evolve when enzymatic activities are targeted on different sites of the fibrinoger/fibrin molecules.…”
Section: Case Reportsmentioning
confidence: 95%
“…The venom and the fibrinolytic fractions degrade fibrin(ogen) in vitro. However, the digestion products obtained are completely different from the plasmin or trypsin digestion products, indicating a different mode of action (6).…”
Section: Introductionmentioning
confidence: 93%
“…Their amino acid sequences exhibit high similarity to other lepidopteran larva serine proteinases [16]. Lonomin II degrades Fg, forming fragments different from those produced by plasmin and trypsin with a very rapid degradation of the ·-chain [17]. These findings may explain the noninhibitory effect of high levels of Fg degradation products found in the patients as demonstrated by total correction of prothrombin time, activated partial thromboplastin time and thrombin time by normal plasma [1,7,8].…”
Section: Anticoagulant Compoundsmentioning
confidence: 99%