Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A new staphylococcal phage, Pphi-2, which could convert the capability of producing staphylokinase, was isolated. The phage is different from the phage reported by Winkler and co-workers [Nature(London) 195:407-408, 1962; J. Gen. Microbiol. 39:321-333, 1965]. The former is a single-converting phage belonging to serotype B, but the latter is a serotype F phage capable of converting not only staphylokinase but also beta-hemolysin. Staphylokinase, i.e., the fibrinolysin produced by Staphylococcus aureus, therefore, can now be classified into three types. One is controlled by the genes on the bacterial chromosome, and the other two are mediated by lysogenic conversion by prophage Pphi-2 and the classical phage reported by Winkler and co-workers.
 ...
PMID:Serotype B staphylococcal bacteriophage singly converting staphylokinase. 14 3

The pesticinogenicity 9.5 kb plasmid from Yersinia pestis strain EV76 has been marked by the kanamycin phosphotransferase gene inserted into PstI site and designated pP3. The obtained plasmid pP3 determines the synthesis of 45 kd pesticin, alpha and beta-forms of fibrinolysin coagulase (37 and 35 kd) and the 29, 19 and 13 kd proteins in Escherichia coli mini cells. When transferred into Yersinia pseudotuberculosis strain 6933 the plasmid causes the proteolysis of outer membrane proteins. The 150 kd protein is reduced to 138 kd, the 48.5 kd protein is reduced to 45 kd. The proteins secreted into the cultural medium (51 and 38 kd) are also cleaved. The proteolysis of the 150 kd protein was found to occur at the stage of secretion via the inner membrane. The purified fibrinolysin coagulase from Escherichia coli strain JM83 harbouring the plasmid pP3 induces the proteolysis in vitro of the isolated membrane proteins from Yersinia pseudotuberculosis strain 6953 similar to the proteolysis registered in vivo.
Mol Gen Mikrobiol Virusol 1991 Jan
PMID:[Specific proteolysis by fibrinolysin-coagulase from Yersinia pestis of Yersinia pseudotuberculosis outer membrane proteins coded by the Ca(2+)-dependence plasmid]. 182 73

The restriction map of Yersinia pestis pesticinogenicity plasmid pYP1 has been constructed with the use of 18 restriction endonucleases. Plasmid dimensions (6.3 Md) have been specified, the genes for pesticin synthesis, for pesticin immunity protein, fibrinolysin and plasmocoagulase have been localized by molecular cloning of single plasmid DNA fragments in vector plasmid pBR322.
Mol Gen Mikrobiol Virusol 1986 Apr
PMID:[Restriction map of pesticinogenicity plasmid pYP1 of Yersinia pestis]. 302 1

The envelope of the bunyavirus La Crosse contains two glycoproteins, G1 (120 000 mol. wt.) and G2 (38 000 mol. wt.). When incubated with trypsin or plasmin, the G1 glycoprotein of virus grown in cell culture was cleaved, leaving two different sized polypeptides in the envelope (67 000 and 95 000 mol. wt.). Chymotrypsin cleaved G1 leaving polypeptides of 70 000 and 100 000 mol. wt. G2, however, was not altered by these enzymes. When used in antibody neutralization studies, these proteolytically modified viruses were neutralized approximately 1 to 2 log10 units in 60 min while control virus was neutralized by over 4 log10 units in 20 min. Because antibody to G1, but not G2, was involved in La Crosse virus neutralization, cleavage of G1 appeared to be directly responsible for these altered kinetics of neutralization. Antibody did bind to the polypeptides remaining associated with the envelope resulting in infectious virus-antibody complexes. This indicated that a critical site in terms of antibody neutralization was removed from G1 by proteolytic enzymes.
J Gen Virol 1983 Oct
PMID:The effect of proteolytic cleavage of La Crosse virus G1 glycoprotein on antibody neutralization. 635 63

Immunochemical identity of Y. pestis fibrinolysin and coagulase is demonstrated using monoclonal antibodies. These substances are proven to exist as complex proteins with two independent activities. Possible causes of this phenomenon are discussed. Coagulase antigenic determinants are involved in specific fluorescence of Y. pestis cells grown at 28 degrees C. A new original method for screening the hybridomas producing monoclonal antibodies is proposed, based on inhibition of the functional activity of antigen.
Mol Gen Mikrobiol Virusol 1999
PMID:[Characterization of Yersinia pestis fibrinolysin using monoclonal antibody]. 1049 79

Acid shift (pH 4.0) of liquid nutrient medium containing 20 mM Mg2+ created conditions in vitro simulating the internal environment of phagolysosome into which Yersinia pestis captured by a macrophage get in vivo. The capacity of Y. pestis to survive and multiply under these conditions irrespective of the plasmid composition of strains was confirmed experimentally. Y. pestis possesses a specific mechanism of fibrinolytic activity inhibition, preventing proteolytic degradation under the effect of Ca-dependent polypeptide (Yops) fibrinolysin and potentiating, in addition to these latter, the production of the so-called "acid" proteins by Y. pestis, coded for by pCad2+ or chromosome, including the potentially new members of LCR family. The culturing conditions affect the length of O-specific lateral chains of Y. pestis lipopolysaccharide (LPS), which corresponds to LPS SR, but not R form.
Mol Gen Mikrobiol Virusol 2001
PMID:[Study of protein and carbohydrate products, synthesized by Yersinia pestis under conditions imitating the internal environment of mammalian phagolysosomal macrophages]. 1181 15

The plasmin-mediated lysis of fibrin present in a wound, or in chronic inflammatory disease, results in the release of fibrin degradation products. One of the two major products is fibrin fragment E, which has been shown to stimulate cell proliferation in many cell types including endothelium, fibroblasts, and smooth muscle cells, and to be angiogenic in the chick chorioallantoic membrane (CAM) system. The activity of fibrin fragment E is dependent on N-terminus thrombin action. Antibodies against fibrin E, which block the cell proliferative activity, were used to locate the active site. Phage epitope display libraries were used to identify the sequence of a peptide, which resembles a region of the N terminus structure. The equivalent synthetic peptide (WTM110) has optimal stimulatory properties at equimolar concentrations to the parent molecule. Such peptide information has therapeutic potential for both stimulating and suppressing angiogenesis and cell proliferation.
Gen Pharmacol 2000 Nov
PMID:Locating the active site for angiogenesis and cell proliferation due to fibrin fragment E with a phage epitope display library. 1188 82

Many of the anomalous results obtained in the fibrinolytic assay of human plasmin systems were shown to be simply explained if bovine plasminogen had been introduced into the assay system on the addition of thrombin. Experimental investigation of the proteolytic and fibrinolytic activity of systems containing plasmin and thrombin showed that enzyme activity was influenced by the presence and quantity of thrombin. The quantity of bovine plasminogen present as a contaminant in bovine fibrinogen was shown to be responsible for only 1/25th of the observed enhanced activity. Thrombin in the amounts commonly used for clotting contained sufficient proenzyme to account for all this activity. A highly purified thrombin preparation obtained from another laboratory, and thrombin purified in this laboratory by starch electrophoresis brought about no enhancement of activity. The material separated from thrombin by starch electrophoresis was shown to be enzymatically identical with bovine plasminogen and, on labelling with radioactive iodine, was shown to behave physically like bovine plasminogen. Several experiments reported in the literature were reinterpreted in the light of this observation.
J Gen Physiol 1957 Jan 20
PMID:The role of a contaminant in thrombin in the human plasmin assay system. 1339 70

Thrombokinase of the blood, while resembling enterokinase in its role of activator, is more closely analogous to trypsin in its intrinsic origin. It probably arises from a plasma precursor; but it is different from plasmin (fibrinolysin). Like trypsin, thrombokinase can activate prothrombin without the aid of other factors; however, it is potentiated by platelets plus calcium. Unlike certain tissue "thromboplastins," it does not sediment appreciably in 2 hours at 85,000 g. Like trypsin, it hydrolyzes p-toluenesulfonylarginine methyl ester (TAMe). Chromatography on DEAE-cellulose separated thrombin from thrombokinase. The TAMe esterase associated with the thrombokinase fractions was largely suppressed by soybean trypsin inhibitor, while that associated with the thrombin fractions was not. Highly purified thrombokinase was used as starting material; and thrombokinase was eluted in the last major protein band. Under these conditions stepwise elution was as effective as gradient in leading to further purification. The product of 199 liters of bovine plasma was chromatographed in 1 day; and the specific activity was comparable to that attained previously by repeated electrophoretic fractionations. The assembled data suggest that the thrombokinase protein may be approaching homogeneity.
J Gen Physiol 1962 Mar
PMID:Thrombokinase of the blood as trypsin-like enzyme. 1403 95

1. Methods for the preparation and partial purification of streptococcal fibrinolysin are described. 2. The lysis of fibrin clots in the presence of streptococcal fibrinolysin is associated with proteolysis of the fibrin. Digestion is due to an enzyme normally present in serum or plasma in an inactive state, which is activated by fibrinolysin. Fibrinolysin alone has no demonstrable proteolytic activity. 3. The lysin factor-fibrinolysin system brings about proteolysis of other proteins such as gelatin or casein, in addition to fibrin and fibrinogen. 4. It is suggested that lysin factor exists in serum or plasma as a zymogen, and that it is activated by fibrinolysin, a kinase, in a manner similar to the activation of trypsinogen by enterokinase or the mold kinase of Kunitz (1938).
J Gen Physiol 1945 Mar 20
PMID:STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN. 1987 27


1 2 Next >>