Results 191 to 200 of about 39,772 (244)

Plasmin-α2-plasmin inhibitor complex and α2-plasmin inhibitor in chronic subdural hematoma

Journal of Neurosurgery, 1989
✓ Levels of the plasmin-α2-plasmin inhibitor complex (PLN-A2PI complex) and α2-plasmin inhibitor (A2PI) were determined by enzyme-linked immunosorbent assay (ELISA) with monoclonal antibodies in 59 patients with 66 chronic subdural hematomas (SDH's). Normal concentrations of the PLN-A2PI complex and A2PI in plasma are below 0.8 µg/ml and 60.5 ± 16.1 µg/
K, Saito, H, Ito, T, Hasegawa, S, Yamamoto   +3 more
openaire   +2 more sources

Fibrinogenolysis by insolubilized plasmin

Clinica Chimica Acta, 1974
Abstract 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.
F R, Matthias, W, Krause, D L, Heene
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Plasmin-α2-antiplasmin complexes (plasmin—plasmin inhibitor complexes)

1999
α2-Antiplasmin (new name: plasmin inhibitor) is the most important plasmin inhibitor. Its rapid reaction with plasmin results in the formation of an inactive complex composed of one molecule of each component. Two steps are involved in this process: first a reversible complex is formed between the lysine-binding sites of plasmin and complementary sites
E. Hattey, M. Haumer, M. R. Griffiths, V. Carroll, B. R. Binder   +4 more
openaire   +1 more source

EXPERIENCE WITH PLASMIN INHIBITORS

Acta Ophthalmologica, 1992
Abstract 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, G B, van Setten, K, Tervo, A, Tarkkanen   +3 more
openaire   +2 more sources

A Standard for Human Plasmin

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, P J, Campbell, P J, Gaffney   +2 more
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Plasmin in subretinal fluid

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, E M, Salonen, A I, Vaheri, L T, Laatikainen   +3 more
openaire   +2 more sources

Fragmentation of Haptoglobin by Plasmin

Canadian Journal of Biochemistry, 1971
Human 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

1993
α2-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, Tetsumei Urano, Yumiko Takada, Akikazu Takada   +3 more
openaire   +1 more source

The plasminogen-plasmin system

Progress in Cardiovascular Diseases, 1991
A 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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Action of Plasmin on Cartilage

Nature, 1958
MUCH 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
openaire   +2 more sources