Results 201 to 210 of about 36,053 (249)
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EXPERIENCE WITH PLASMIN INHIBITORS
Acta Ophthalmologica, 1992Abstract The involvement and role of the plasmino‐gen activator‐plasmin system in normal and pathological wound healing is reviewed. The methods currently available for demonstrating plasmin activity are briefly described. The article also reviews some other serine proteases potentially involved in pathological wound healing processes.
T, Tervo +3 more
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Thrombosis and Haemostasis, 1975
SummaryAn international collaborative study involving ten laboratories was undertaken to assess the suitability of a preparation of human plasmin in 50% glycerol to serve as a single standard for the bioassay of plasmin activity. The study included examination of the stability of the proposed standard and comparisons between assay methods.
T B, Kirkwood +2 more
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SummaryAn international collaborative study involving ten laboratories was undertaken to assess the suitability of a preparation of human plasmin in 50% glycerol to serve as a single standard for the bioassay of plasmin activity. The study included examination of the stability of the proposed standard and comparisons between assay methods.
T B, Kirkwood +2 more
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Acta Ophthalmologica, 1988
Abstract. Proteolytic activity was studied in subretinal fluid from 56 eyes with rhegmatogenous retinal detachment without vitreous or subretinal hemorrhage. Active plasmin (1.0–15.2 μg/ml) was found in 33 eyes and plasmin‐inhibitor complexes in 3 eyes.
I J, Immonen +3 more
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Abstract. Proteolytic activity was studied in subretinal fluid from 56 eyes with rhegmatogenous retinal detachment without vitreous or subretinal hemorrhage. Active plasmin (1.0–15.2 μg/ml) was found in 33 eyes and plasmin‐inhibitor complexes in 3 eyes.
I J, Immonen +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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Fragmentation of Haptoglobin by Plasmin
Canadian Journal of Biochemistry, 1971Human haptoglobin type Hp 1-1, is hydrolyzed by plasmin to give two dissimilar products, P1 and P2, with molecular weights of 78 000 and 17 000, respectively. The larger fragment, P1 has the same N-terminal amino acids, valine and isoleucine, as intact haptoglobin.
F, Ofosu, D W, Campbell, G E, Connell
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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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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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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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