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- W1981102616 abstract "The anticoagulant actions of the basic phospholipases A (PLA) from snake venoms were stronger than those of the neutral or acidic phospholipases A, and their enzymatic activities were not parallel with their anticoagulant activities. When the enzymatic activity of Trimeresurus mucrosquamatus snake venom phospholipase A (TMV-PLA) was almost completely (>99%) inhibited with p-bromophenacyl bromide, the anticoagulant activity was decreased markedly. The procoagulant activity of lysocephalin, derived from cephalin by the action of phospholipase A, was only about one hundredth of that of cephalin. When p-bromophenacyl bromide-modified TMV-PLA was added to the mixture of cephalin and lysocephalin, it still could prolong the Stypven clotting time. The anticoagulant activity of TMV-PLA may be due to both enzymatic and binding activities. The anticoagulant activity of Naja naja atra snake venom phospholipase A (NNAV-PLA) was very weak in the presence of plasma and cephalin. However, when NNAV-PLA was preincubated with cephalin at 37°C for 2 min and then plasma was added to this preincubation mixture, the anticoagulant effect of NNAV-PLA was more marked. This indicated that the weak anticoagulant activity of NNAV-PLA was due to interference of phospholipid binding to NNAV-PLA by plasma binding proteins. The phospholipid-binding activity of PLA is thought to be a prerequisite for its anticoagulant activity, with the enzymatic activity potentiating its anticoagulant activity. The anticoagulant activity of basic PLA was usually stronger than that of acidic PLA, possibly due to stronger binding activity." @default.
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- W1981102616 date "1981-01-01" @default.
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- W1981102616 title "Mechanism of the anticoagulant action of phospholipase A purified from Trimeresurus mucrosouamatus (Formosan habu) snake venom" @default.
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- W1981102616 doi "https://doi.org/10.1016/0041-0101(81)90123-9" @default.
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