Results 241 to 250 of about 63,107 (284)
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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.
Ilkka J. R. Immonenm +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.
Ilkka J. R. Immonenm +3 more
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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.
Gysbert-Botho van Setten +3 more
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Fibrinogenolysis by insolubilized plasmin
Clinica Chimica Acta, 1974Abstract Insolubilized plasmin was prepared by chemical fixation of the enzyme to CNBr-activated agarose. The enzyme is still active, whereas its specific activity is reduced. Fibrinogenolysis by insolubilized plasmin is compared to fibrinogenolysis by the soluble form of the enzyme.
Dieter L. Heene +2 more
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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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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 ...
Akikazu Takada +3 more
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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 ...
Charles H. Lack, H. J. Rogers
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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.
Heechung Yang +2 more
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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.
Akiko Hijikata +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.
H. D. Anderson +4 more
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THE ACTIVATION AND DETERMINATION OF PLASMIN IN THE RAT [PDF]
Canadian Journal of Biochemistry and Physiology, 1959 The presence of a proteolytic enzyme precursor (plasminogen) in the euglobulin fraction of rat plasma was demonstrated and optimum conditions for its activation and determination were studied. Rat plasmin activity was estimated (casein-digestion method) following activation of the enzyme with streptokinase-activated human serum euglobulin under various
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