Results 161 to 170 of about 30,314 (207)
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The Dissociation of α2-Plasmin-Inhibitor-Plasmin Complex to Active Plasmin by SDS Treatment
1993α2-PI has been demonstrated to be the physiologically most important inhibitor to plas. sin in plasma [1–3], it is a single-chain glycoprotein with molecular weight of about 68,000 [2,4] and inhibits proteolytic activity of plasmin by forming a 1:1 stoichiometric complex which is enzymatically inactive and hardly dissociated by dodecyl sulfate under ...
Dong Yan +3 more
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The plasminogen-plasmin system
Progress in Cardiovascular Diseases, 1991A REVIEW of the literature of plasminogen (Pg) and plasmin (Pm) encompasses many fields of research. Studies of physical biochemistry, enzyme kinetics and mechanism, enzyme inhibitors, human genetics and physiological regulation of enzymatic activities are but a few of the relevant topics.
J, Henkin, P, Marcotte, H C, Yang
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Plasmin inactivation in Plasma
Thrombosis and Haemostasis, 1976SummaryInhibition and inactivation of plasmin is ascribed to α2-macroglobulin, α1-antitrypsin and c1-esterase inhibitor. In an “overall” inactivation test of plasmin in plasma, which comes perhaps closest to rapid inactivation of plasmin in the circulating blood, we only found a correlation between the immunological concentration of α2-macroglobulin ...
E M, Haselager, T M, Goote, J, Vreeken
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Biochimica et Biophysica Acta, 1960
Abstract Plots of the variation of p K m and log V max with pH for plasmin, determined in the absence and presence of either Ni ++ or Ca ++ , indicate that the active center of this enzyme is functionally identical to trypsin and that both of these enzymes differ significantly from thrombin.
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Abstract Plots of the variation of p K m and log V max with pH for plasmin, determined in the absence and presence of either Ni ++ or Ca ++ , indicate that the active center of this enzyme is functionally identical to trypsin and that both of these enzymes differ significantly from thrombin.
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Action of Plasmin on Cartilage
Nature, 1958MUCH recent work1–4 has shown that a considerable proportion of the chondroitin sulphate in the ground substance of cartilage is combined in some way or other with protein. It is possible that the relative ease with which the mucopolysaccharide can be obtained in a protein-free form5 by extraction with mild alkali is a reflexion of the alkali lability ...
C H, LACK, H J, ROGERS
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Canadian Journal of Biochemistry and Physiology, 1962
Several aspects of the properties and preparation of human plasmin are considered. It appears that glycerol activation of the proenzyme is a peculiar property dependent in part on the structure of the glycerol molecule since closely related compounds are without effect.
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Several aspects of the properties and preparation of human plasmin are considered. It appears that glycerol activation of the proenzyme is a peculiar property dependent in part on the structure of the glycerol molecule since closely related compounds are without effect.
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Synthesis of plasmin substrates and relationship between their structure and plasmin activity
International Journal of Peptide and Protein Research, 1986The plasmin substrates, D‐Ile‐Phe‐Lys‐pNA (I), 3‐MV‐Phe‐Lys‐pNA (II), Ile‐Phe‐Lys‐pNA (III), D‐Pro‐Phe‐Lys‐pNA (IV), CP‐Phe‐Lys‐pNA (V) and Pro‐Phe‐Lys‐pNA (VI), were synthesized by the conventional solution method and the kinetic parameters of their amidolysis by plasmin were determined.
Y, Okada +7 more
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The Preparation of Human Fibrinolysin (Plasmin)
Vox Sanguinis, 1960SummaryTo date, methods reported for purifying human profibrinolysin have given erratic yields and purities. A versatile method is described for purification which can be used with most preparations of Fraction III from human plasma. This method results in a good yield of a highly purified profibrinolysin.
J T, SGOURIS +4 more
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Assessing Plasmin Generation in Health and Disease
International Journal of Molecular Sciences, 2021Adam Miszta +2 more
exaly