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Y Tamaura

Publications and source records attributed to Y Tamaura.

13 recordsLinked to original sources
PubMed1979

Fibrin suspension as a substrate fop plasmin: determination and kinetics.

Fibrin polymers formed from fibrinogen with thrombin in the presence of EDTA were suspended in a medium containing glucose, arabic gum and imidazole-HCl buffer and were sonicated at 20 kHz for 20 min to make a suspension containing fibrin particles of small size. The fibrin suspension was used as a substrate of plasmin for determining the enzymic activity of plasmin and plasminogen activated with urokinase. The kinetic study on the reaction of the fibrin particles with plasmin in the presence and the absence of fibrinogen revealed that Km value of fibrin for plasmin is 4.2 x 10(-7) M and the Ki value of fibrinogen is 1.2 x 10(-5) M.

Electrophoresis, Disc↗
PubMed1979

Inhibition of E coli ATPase activity by a troponin component, TN-I, and by mitochondrial ATPase inhibitor.

The enzymic activity of Mg2+- or Ca2+-stimulated ATPase from Escherichia coli was inhibited by one of the troponin components, TN-I, and by mitochondrial ATPase inhibitor (F1-inhibitor). The inhibitory ability of component TN-I against Mg2+-stimulated AtPase activity was lost after digestion of component TN-I with trypsin. The Mg2+-stimulated ATPase activity inhibited by component TN-I was completely restored by the addition of another troponin component TN-C.

Adenosine Triphosphatases↗
PubMed1978

Faster determination of clottable fibrinogen in human plasma: an improved method and kinetic study.

Clottable fibrinogen in human plasma was determined by measuring spectrophotometrically the increase in turbidity with time due to the fibrinogen-fibrin conversion with thrombin. From the maximal absorbance, Amax, at 450 nm obtained 2 min or less after thrombin as added to plasma, we estimated the fibrinogen concentration in plasma of normal subjects and patients. Analysis of the rate of the absorbance increase yielded the Km value, 1.6 X 10(-5) mol/liter, which closely agrees with the Km of 1.2 X 10(-5) mol/liter obtained by analysis of the fibrinopeptides released from fibrinogen.

Fibrinogen↗