Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.5 (thrombin)
 33,306 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Heparin binding on polymorphonuclear leucocytes (PMNL) was characterized. Heparin binding was specific, rapid, saturable and reversible. One single class of heparin binding sites was found with a dissociation constant of 1.22 mumol/l and 7.7 x 10(6) sites per PMNL. The binding was independent of the anticoagulant activity of heparin. Heparin affinity chromatography on radio-iodinated cell lysates followed by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulphate revealed a 130 kD heparin binding protein. Heparin binding was inhibited by disodium salt of ethylenediamine tetraacetic acid. Cell surface bound heparin was functionally inactive and did not affect the inactivation of thrombin by antithrombin III. Our study demonstrates that heparin interacts with PMNL by a cell-surface binding protein. These instructions could be consistent with the modifications of some PMNL functional properties in the presence of heparin.
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PMID:Specific binding between human neutrophils and heparin. 152 Jun 30

Interaction of fractionated 3H-heparin with plasma proteins was investigated by gel filtration chromatography. The peak of the elution profile for fractionated 3H-heparin in rat plasma was observed at the higher molecular weight fraction than that for fractionated 3H-heparin in buffer without any protein, suggesting the existence of fractionated 3H-heparin binding protein(s) in plasma. Then the interaction of fractionated 3H-heparin with such plasma proteins as albumin, antithrombin III, thrombin and alpha-globulin was investigated. The elution profile for fractionated 3H-heparin in albumin solution, antithrombin III solution and the solution containing antithrombin III and thrombin were different from that for fractionated 3H-heparin in plasma. The elution profile for fractionated 3H-heparin in alpha-globulin solution, of a concentration close to that in plasma, was comparable to that of fractionated 3H-heparin in plasma, though two peaks were found. The major peak corresponded to that of fractionated 3H-heparin in plasma, and the minor peak eluted at a higher molecular weight fraction. When alpha-globulin concentration was decreased, the major peak shifted to the lower molecular weight fraction, and the minor peak was diminished and then disappeared. Thus it was suggested that alpha-globulin is dominant for plasma protein binding of fractionated 3H-heparin.
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PMID:Investigation on interaction of fractionated 3H-heparin with plasma proteins by gel filtration chromatography. 248 Apr 40