Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

When Glu-plasminogen (Glu-plg) was incubated with plasmin for various time intervals, and the mixture was activated by urokinase (UK), the activation rate increased gradually as incubation time increased. The presence of fibrin not only enhanced the activation rate of Glu-plg but also that of proteolytically modified form to some extent. The results of SDS-PAGE indicated that the release of N-terminal peptides from Glu-plg or Glu-plasmin takes place gradually when the concentration of plg was about 1 microM, and that Glu-plasmin I of larger molecular weight is more slowly converted to Lys-plasmin than Glu-plasmin II of smaller molecular weight. The amounts of carbohydrate moieties on the heavy chain of plasmin may influence the release of N-terminal peptide from Glu-plasmin. Kinetic studies indicate that Lys-plasmin has smaller km than Glu-plasmin, thus the former being better enzymatically than the latter.
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PMID:Activation pathway of glu-plasminogen to Lys-plasmin by urokinase. 612 17

The presence of soluble fibrin complexes (SFC) measured by gel filtration of plasma on 4% agarose columns, fibrinogen heterogeneity on 3.5% SDS-polyacrylamide gels and the concentrations of several plasma proteins were evaluated in 39 patients with diabetes mellitus (DM) and 19 matched control subjects. A small but significant increase of SFC was found in DM (p less than 0.01). On individual basis 51.2% of the patients had increased SFC (greater than M + 2 SD of the controls). Polyacrylamide gel electrophoresis of the SFC showed no evidence of cross-linking or proteolysis. Plasma clots formed in the presence of EDTA and trasylol were analysed in SDS-polyacrylamide gels in a normal and two lower molecular weight fibrin bands (band I, II, III). The percentage of band I fibrinogen was in diabetics (65.3 +/- 4.7%) lower than that of the controls (71.8 +/- 4.5%) (p less than 0.01). Fibrinogen levels, antithrombin III, alpha 1-antitrypsin, alpha 2-macroglobulin and plasminogen were significantly increased in DM. We suggest that in DM there is an enhancement of intravascular fibrin formation and accelerated fibrinogen degradation to lower molecular weight forms.
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PMID:Soluble fibrin complexes and fibrinogen heterogeneity in diabetes mellitus. 616 8

Porcine tissue-type plasminogen activator (t-PA) increases the binding of 125I-glu-plasminogen to clots made from human plasma or purified fibrinogen in a time and t-PA concentration dependent fashion. The accumulation of plasminogen was faster and greater on noncrosslinked plasma clots than on clots which had been crosslinked by Factor XIIIa. Furthermore, the uptake of plasminogen to crosslinked fibrin clots occurred at a slower rate in the presence of alpha 2-plasmin inhibitor (alpha 2 PI) than in its absence. The kinetics of the uptake of 125I-plasminogen were analyzed using SDS-polyacrylamide gel electrophoresis and radioautography of solubilized plasma clots formed in the presence of t-PA. During the initial phase there was a decrease of clot-bound glu-plasminogen; simultaneously, there was a slight increase in clot-bound glu-plasmin and in plasmin complexed to alpha 2 PI that was crosslinked to alpha-chain polymers of fibrin. This was followed by a marked increase in clot-bound plasminogen having glutamic acid as NH2-terminal (glu-plasminogen) and gluplasmin. t-PA-induced enhancement of glu-plasminogen uptake appears to be mediated by plasmin but does not require the conversion of glu-plasminogen to plasminogen having lysine or methionine as NH2-terminal. The described mechanism assures an adequate supply of clot-bound plasmin, which is the enzyme ultimately involved in the degradation of fibrin.
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PMID:Tissue-type plasminogen activator increases the binding of glu-plasminogen to clots. 621 Mar 7

Triton X-100 and NaSCN extracts of 18 normal breast and colon tissues and of 20 breast and colon carcinomas were fractionated by SDS-PAGE and plasminogen activators (PA) revealed by a zymographic method. Four different lysis bands, corresponding to MWs of 54,000, 68,000, 95,000 and 110,000 were observed. Using immunoadsorption with specific antisera against urokinase (UK) and tissue PA (t-PA), we found that all normal tissue extracts contained free t-PA (68 kd). Some of these revealed, in addition, a complex (110 kd) of t-PA with a 40-kd component. The latter presumably represents the fast-acting specific inhibitor of t-PA and UK. Most carcinoma extracts contained, in addition to the two t-PA-related lysis bands, the UK-related 54 kd PA, and some a 95 kd complex of UK with the 40 kd component. For each extractant, mean total fibrinolytic activity of normal and tumor tissue was comparable when measured on conventional fibrin plates, but breast and colon carcinomas contained higher concentrations of UK-related PA. PA activity was higher in normal and carcinoma NaSCN extracts than in the corresponding Triton X-100 extracts. In general, Triton X-100 but not NaSCN extracts of malignant tissue contained a high concentration of fibrinolytic inhibitors. Mixing experiments revealed that the inhibitory activity was mainly directed against UK. It was abolished by acidification of the carcinoma extracts. The anti-UK inhibitory activity was absent in extracts of normal breast or colon and appears to be different from the 40 kd fast-acting PA inhibitor. These studies show that malignant transformation of breast and colon is accompanied by important changes of the production of a UK-related PA and of an inhibitory activity directed against UK.
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PMID:Characterization of plasminogen activators from normal human breast and colon and from breast and colon carcinomas. 623 65

On the basis of cellular morphology, a subline of mouse sarcoma virus-infected 3T3 cells was selected which released a 48 000-dalton plasminogen activator at an approx. 40-fold higher rate than those of the parent line, and which continued to do so for several months when the cells were maintained in serum-free culture medium. Culture medium (3.5 l) containing 0.6 mg plasminogen activator per l was used to purify 620 micrograms of the enzyme 130-fold with a yield of 32% by affinity chromatography followed by anion exchange chromatography and gel filtration. Crucial for the yield was the use of a non-ionic detergent and of inhibitors of proteolysis to prevent adsorption and degradation, respectively. The purified enzyme was homogeneous as evaluated by SDS-polyacrylamide gel electrophoresis and had an isoelectric point of pH 9.2. The purified enzyme showed characteristics of a trypsin-like serine protease (labeling with [3H]diisopropylphosphorofluoridate which was prevented by p-nitrophenyl-p'-guanidinobenzoate) and converted the single chain of human plasminogen into two chains of plasmin with electrophoretic mobilities identical to those of the chains formed by non-purified enzyme and by human urokinase. In the absence of inhibitors, solutions of purified enzyme were stable for 24 h at 4 degrees C at pH 3-9.
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PMID:Purification and characterization of a plasminogen activator from mouse cells transformed by an oncogenic virus. 625 3

Electrophoretic analysis of plasminogen activators from pig heart, human uterus, human plasma and human melanoma cells was performed in SDS-polyacrylamide gradient slab gels containing plasminogen and casein. Direct visualization of activator activity bands in polyacrylamide gels was achieved after removal of SDS, incubation in buffer, and staining with Coomassie brilliant blue. Tissue activator extracted from pig hearts displayed a molecular weight of 72000 and migrated similarly to activator secreted by human melanoma cells and to one activator component present in extracts of human uterus. Immunoadsorption experiments with melanoma cell activator antiserum indicated that these 72-kDa activators are all related immunologically. Human uterus also contained a second activator component with a molecular weight 55000, which migrated similarly to a higher molecular weight component of urokinase and cross-reacted with urokinase antiserum. We conclude that the 72-kDa uterine activator component represents a tissue activator and the 55-kDa component represents a urokinase-like activator. A euglobulin solution from venous occlusion plasma displayed multiple bands of plasmin activity in the Mr range 85000-96000. Two activator components were also present, one of Mr 72000 and another of Mr 62000. The 72-kDa euglobulin activator was adsorbed by MCA antiserum, and we conclude that this component represents vascular activator. The 62000 activator also had weak plasminogen-independent caseinolytic activity and was not affected by either melanoma cell activator or urokinase antisera. Conclusions concerning its identity cannot be made at this time.
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PMID:Comparative electrophoretic analysis of human and porcine plasminogen activators in SDS-polyacrylamide gels containing plasminogen and casein. 634 80

Glu-plasminogen (Glu-plg) was eluted through lysine-Sepharose by using a gradient of 6 aminohexanoic acid, and two peaks corresponding to Glu-plg I and II were obtained. Glu-plg I has a molecular weight of 93,000 and Glu-plg II has a molecular weight of 89,000. When these plgs were activated by urokinase (UK) or streptokinase (SK) in the presence of S-2251 (H-D-Val-Leu-Lys-pNA0, the hydrolysis of S-2251 by Glu-plg I activated by UK or SK was larger than that by Glu-plg II activated by UK or SK. The results of SDS-PAGE indicate that the conversion of Glu-plg I to plasmin by UK was faster than that of Glu-plg II. It may be concluded that Glu-plg I is activated better to plasmin by activators than Glu-plg II.
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PMID:The activation of two isozymes of glu-plasminogen (I and II) by urokinase and streptokinase. 635 45

Electrophoresis of cornified cell extracts of 2-day-old rats, using SDS polyacrylamide gels copolymerized with alpha-casein or gelatin with or without plasminogen, was performed. Both Tris-HCl buffer soluble protein and KSCN solubilized protein contained a number of hydrolases for alpha-casein and/or gelatin, but PA (mol. wts 57 and 50K) was found only in the KSCN extract. The pH dependency, substrate specificity and mol. wt of plasminogen-independent proteinases were comparatively determined and DFP inhibition tested. This simple technique helped to identify the presence of several proteinases and to characterize them in partially purified epidermal extracts.
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PMID:Detection and characterization of epidermal proteinases by polyacrylamide gel electrophoresis. 636 28

The plasminogen activator (PA) produced by freshly purified human monocytes-macrophages and histiocytic, lymphoma-derived U 937 cells was analyzed by zymography after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and found to migrate with an apparent Mr of 55,000, identical to that of urokinase (Uk). By immunoprecipitation with antibodies specific for the two different types of PA, the enzyme was shown to be immunologically related to urokinase, and not to tissue PA. Urokinase was secreted in the form of the inactive Mr 55,000 zymogen prourokinase , and could be converted to the active Mr 55,000 enzyme by limited proteolysis with plasmin. Conditioned media from cultures of U 937 cells and monocytes-macrophages inhibited the fibrinolytic activity of exogenously added urokinase. Using [125I]-labeled urokinase we observed the formation of an enzyme-ligand complex, which was not dissociated by boiling in SDS and migrated with an apparent Mr 40,000 daltons higher than the free enzyme; since complexed urokinase was functionally inactivated as a PA, the ligand is an inhibitor of urokinase. This inhibitor is different from fibroblast-produced protease- nexin , in that it did not interact with thrombin. These results suggest that plasminogen activation by mononuclear phagocytes can be modulated through the secretion of both (pro)enzyme and a specific inhibitor.
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PMID:Concomitant secretion of prourokinase and of a plasminogen activator-specific inhibitor by cultured human monocytes-macrophages. 637 11

A new method is described for the preparation of highly purified human plasminogen and plasmin with specific activity of 32 CTA units per mg of protein. With this method, the purification of the urinary plasminogen + plasmin antigenic materials from patients with chronic glomerulonephritis, disseminated intravascular coagulation syndrome and severe toxemia of pregnancy was performed, and the resulting highly purified proenzyme and enzyme were analyzed by immunoelectrophoresis, separative agar electrophoresis, gel filtration and SDS-gel electrophoresis. Our findings indicated that urinary plasmin reflects more closely the extent of intraglomerular fibrinolysis, while urinary plasminogen reflects non-selective proteinuria in patients with chronic glomerulonephritis or severe toxemia of pregnancy.
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PMID:Studies on the purification and characterization of human urinary plasminogen and plasmin. 644 89


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