Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Up to 50% of [35S]-heparin molecules prepared from rat skin bind to rabbit muscle myosin ATPase, in a concentration dependent manner, producing a stable complex with a dissociation constant of 3 x 10(-7) M. The [35S]-heparin in the complex has a distinct electrophoretic behaviour and is precipitated by TCA together with myosin. Other [35S]-glycosaminoglycans, namely, heparan sulfate, dermatan sulfate and chondroitin sulfate also prepared from rat tissues are unable to form complexes with the enzyme. Among the sulfated glycosaminoglycans obtained from different sources only heparin is able to displace the bound [35S]-heparin from the ATPase. Heparin with high affinity for antithrombin III, prepared by antithrombin-affinity chromatography, dislodges up to 90% of the bound [35S]-heparin. Furthermore, antithrombin III-high affinity heparin shows a high affinity for myosin ATPase when compared to antithrombin III-low affinity heparin which shows a low affinity for the enzyme. It is also shown that myosin ATPase inhibits the "in vitro" plasma anticoagulant activity of heparin. These are suggestive that the special structure of the heparin molecules needed for the binding to antithrombin and myosin ATPase bears important similarities. The mechanism of the hemorrhagic effect of heparin is discussed in view of these interactions.
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PMID:Interaction of heparin with myosin ATPase: possible involvement with the hemorrhagic activity and a correlation with antithrombin III high affinity-heparin molecules. 147 Oct 71

Heparin and its fragments, namely, trisulfated disaccharide, pentasulfated tetrasaccharide, octasulfated hexasaccharide and an oligosaccharide (M.W. 6,300) prepared by enzymatic fragmentation and an oligosaccharide (M.W. 4,500) prepared by chemical fragmentation are potent inhibitors of skin hemostasis when applied topically. All the heparin fragments tested are 10 to 20 times more active than heparin itself on a weight basis in disrupting the normal hemostatic mechanism. As heparin, the fragments produce a residual antihemostatic effect which persists after extensive washing of the preparation with isotonic solutions. This residual effect could be removed either by ATP or myosin ATPase.
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PMID:Antihemostatic activity of heparin disaccharides and oligosaccharides obtained by chemical and enzymatic fragmentation: reversal of the hemorrhagic activity by ATP and myosin. 274 12