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M C Guillin

Publications and source records attributed to M C Guillin.

71 records · Page 4Linked to original sources
PubMed1985

[Thrombopenia].

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Hematologic Tests↗
PubMed1985

[General mechanisms of coagulation and their physiological inhibition. I. General mechanisms of blood coagulation].

Blood coagulation results from a sequence of enzymatic reactions, which involve 12 plasma proteins (coagulation factors), platelets, a tissue lipoprotein (tissue factor), vascular components and calcium ions. These reactions are induced by vascular lesions, and are promoted by blood contact with sub-endothelial structures and by the release of tissue factor into the circulation; they result in the formation of an hemostatic plug constituted of platelets and fibrin. The enzymatic reactions consist of proteolytic reactions, in which zymogens are converted to proteinases. These reactions are accelerated by both proteins-proteins interactions and by proteins-membrane surface (vascular wall, platelets) interactions, responsible for the amplification of the activation process, and its localization at the site of injury. The coagulation process is regulated by positive and negative feed-backs and by physiological inhibitors.

Animals↗
PubMed1984

Prothrombin Salakta: an abnormal prothrombin characterized by a defect in the active site of thrombin.

An abnormal prothrombin has been detected in a 17 yr-old female originating from Tunisia. There was no history of excessive bleeding. Prothrombin time and activated partial thromboplastin time were moderately prolonged. Prothrombin activity was 15-18% when measured using either the classical one-stage and two-stage assays, or assays with Echis carinatus venom or staphylocoagulase, whereas prothrombin antigen was 100%. In keeping with current nomenclature practices, the abnormal molecule has been designated prothrombin Salakta. The electrophoretic behaviour and calcium binding properties of the abnormal prothrombin did not differ significantly from normal, as assessed by crossed immunoelectrophoresis. Prothrombin Salakta was isolated by chromatography on DEAE-Sephadex and Dextran sulphate sepharose. Electrophoretic migration of purified prothrombin Salakta on SDS polyacrylamide gels or alkaline disc gels was normal. Upon activation by either bovine factor Xa or Echis carinatus venom, thrombin activity produced by prothrombin Salakta was only 15% of normal, even when the incubation period was prolonged for 24 hours. The pattern of factor Xa-catalyzed proteolysis of prothrombin Salakta, investigated by SDS polyacrylamide gel electrophoresis, was found to be normal. These results indicated that prothrombin Salakta was characterized by a defective thrombin enzymatic activity. Thrombin Salakta was therefore isolated by heparin-sepharose chromatography. Affinity for heparin and molecular weight of thrombin Salakta were found to be normal. Biological activity of thrombin Salakta, determined by clotting assay, was 535 u/mg versus 3 200 u/mg for normal thrombin. Amidolytic activity of thrombin Salakta parallelled its clotting activity, suggesting that the defect resides either in the catalytic site or in the residues adjacent to the catalytic site and implicated as contact residues, rather than in the fibrinogen recognition site.

Adolescent↗
PubMed1984

Quantitation of prothrombin activation products in human urine.

Urine samples obtained from 37 normal individuals have been screened for the presence of prothrombin activation products using radioimmunoassays developed for fragment 1, fragment 2 and prothrombin derivatives bearing the thrombin region. The cross-reacting materials detected in urine were isolated by affinity chromatography on insolubilized antibodies, and analysed by SDS polyacrylamide gel electrophoresis. The only prothrombin derivatives detected were fragment 1 (37/37) and fragment 2 (22/37). The mean values of daily urinary fragment 1 and fragment 2 excretion were respectively 13.4 nM and 1.5 nM. The excretion of prothrombin derivatives has been quantitated in 14 normal pregnant women, during the third trimester of gestation. The mean values of urinary excretion were 47.2 nM per day for fragment 1 (P less than 0.005) and 6.4 nM per day for fragment 2 (P less than 0.05). The significant increase in fragment 1 and fragment 2 excretion observed in a condition known to be associated with the so-called hypercoagulable state suggest that the measurement of prothrombin derivatives in urine could be a useful tool for the non-invasive detection of thromboembolic diseases or prethrombotic states.

Adolescent↗
PubMed1978

The mechanism of activation of human prothrombin by an activator isolated from Dispholidus typus venom.

Purified human prothrombin was activated, both in the absence and in the presence of thrombin inhibitors (diisopropylfluorophosphate or hirudin), by a coagulant principle isolated from Dispholidus typus venom. The process of activation was monitored by sodium dodecyl sulfate polyacrylamide gel electrophoresis. In the absence of thrombin inhibitor, prolonged incubation of prothrombin with the purified venom yielded thrombin, fragment 1 (F 1) and fragment 2 (F 2). In the presence of diisopropylfluorophosphate, which in the experimental conditions used inhibited only partially the thrombin generated activity, products obtained upon activation of prothrombin by venom were F 1 and a two-chain, disulfide-bridged protein of 58 000 daltons called meizothrombin (des F 1). In the presence of hirudin, which fully inhibited thrombin generated activity, prothrombin activation by the venom did not liberate any fragment, but prothrombin was converted to a derivative composed of two disulfide-bridged polypeptide chains of 48 000 and 37 000 daltons, called meizothrombin. These results are similar to those reported by others when studying the process of prothrombin activation by Echis carinatus venom and allow to conclude that Dispholidus typus venom cleaves a bond linking the A and B chains of thrombin, converting prothrombin into meizothrombin. This enzyme is then responsible for the cleavage of the bond linking F 1 and F 2 and the bond linking F2 the A chain of thrombin.

Animals↗