The Kidney and Fibrinolysis

1970 ◽  
Vol 24 (01/02) ◽  
pp. 026-032 ◽  
Author(s):  
N. A Marsh
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Enzyme System ◽  
Normal Animal ◽  
Fibrinolytic Enzyme ◽  
The Other ◽  
Exclusion Chromatography ◽  
Normal Urine ◽  
Renal Origin ◽  
Molecular Exclusion Chromatography

SummaryMolecular exclusion chromatography was performed on samples of urine from normal and aminonucleoside nephrotic rats. Normal urine contained 2 peaks of urokinase activity, one having a molecular weight of 22,000 and the other around 200,000. Nephrotic urine contained three peaks of activity with MW’s 126,000, 60,000 and 30,000. Plasma activator determined from euglobulin precipitate had a MW. in excess of 200,000. The results indicate that in the normal animal, plasma plasminogen activator does not escape into the urine in substantial quantities but under the conditions of extreme proteinuria there may be some loss through the kidney. The alteration in urokinase output in nephrotic animals indicates a greatly disordered renal fibrinolytic enzyme system.The findings of this study largely support the hypothesis that plasma plasminogen activator of renal origin and urinary plasminogen activator (urokinase) are different molecular species.

Arterio-Venous Differences in the Components of the Fibrinolytic Enzyme System

1966 ◽  
Vol 16 (01/02) ◽  
pp. 032-037 ◽  
Author(s):  
D Ogston ◽  
C. M Ogston ◽  
N. B Bennett
Keyword(s):  
Plasminogen Activator ◽  
Enzyme System ◽  
Venous Blood ◽  
Fibrinolytic Enzyme ◽  
Blood Levels ◽  
Activator Concentration ◽  
Blood Samples ◽  
Arterial Blood ◽  
Male Subjects

Summary1. The concentration of the major components of the fibrinolytic enzyme system was compared in venous and arterial blood samples from male subjects.2. The plasminogen activator concentration was higher in venous blood and the arterio-venous difference increased as its concentration rose, but the ratio of the arterial to venous level remained constant.3. No arterio-venous difference was found for anti-urokinase activity, antiplasmin, plasminogen and fibrinogen.4. It is concluded that venous blood determinations of the components of the fibrinolytic enzyme system reflect satisfactorily arterial blood levels.

Effect of muscular exercise in a hot environment on canine fibrinolytic activity

1965 ◽  
Vol 20 (6) ◽  
pp. 1307-1311 ◽  
Author(s):  
E. Bedrak
Keyword(s):  
Heat Stress ◽  
Plasminogen Activator ◽  
Fibrinolytic Activity ◽  
Enzyme System ◽  
Fibrinolytic Enzyme ◽  
Plasma Fibrinogen ◽  
Muscular Exercise ◽  
Heat Acclimatization ◽  
Hot Environment ◽  
Fibrin Plate

The effect of muscular exercise, heat stress, and muscular exercise plus heat stress on the euglobulin fibrinolytic enzyme system was determined in 11 Alsatian dogs prior to and after acclimatization in a hot environment. All the physiological stresses employed, particularly muscular exercise in a hot environment, enhanced the fibrinolytic activity and lowered plasma fibrinogen levels in all animals, especially in the nonacclimatized. The increased fibrinolytic activity, as measured by fibrin plate methods, was primarily related to plasminogen activator and to a lesser degree to active plasmin. In acclimatized animals at rest, the activity of plasminogen activator is lower, that of plasmin is relatively unchanged, while the level of plasma fibrinogen tends to be higher than in nonacclimatized animals at rest. euglobulin fibrinolytic activity and heat acclimatization in dogs; heat stress; plasminogen activator; plasmin fibrinogen and heat acclimatization; nonacclimatized and heat-acclimatized dogs Submitted on November 23, 1964

scholarly journals The xylanase system of Coniophora cerebella

1968 ◽  
Vol 108 (4) ◽  
pp. 571-576 ◽  
Author(s):  
N. J. King ◽  
D. B. Fuller
Keyword(s):  
Molecular Weight ◽  
Culture Filtrate ◽  
Uronic Acid ◽  
Enzyme System ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
The Other ◽  
Xylose Residue ◽  
Random Manner ◽  
Acidic Sugars

1. The culture filtrate of the fungus Coniophora cerebella grown on poplar 4-O-methylglucuronoxylan as carbon source and enzyme inducer contained an enzyme system that degraded the polysaccharide to xylose, acidic and neutral oligosaccharides and an enzyme-resistant polymer. Free uronic acid was not produced. 2. Cold ethanol fractionation of the culture filtrate yielded two active fractions, one of which had only xylanase (EC 3.2.1.8) and the other both xylanase and xylosidase (EC 3.2.1.37) activities. Further fractionation on DEAE-cellulose resolved the xylanase and xylosidase activities. 3. The xylanase degraded poplar 4-O-methylglucuronoxylan in an essentially random manner, producing oligosaccharides, but some xylose residues in the vicinity of uronic acid side groups were protected from hydrolysis, preventing a truly random attack. The xylosidase attacked the polysaccharide very slowly, releasing xylose, but the oligosaccharides produced by the action of the xylanase were much more susceptible to hydrolysis by the xylosidase. 4. The products of xylanase action were separated into neutral and acidic fractions. The neutral oligosaccharides were separated by chromatography on charcoal–Celite, and the major products were characterized as xylobiose, xylotriose, xylotetraose and xylopentaose. Some of the acidic sugars were branched, having the uronic acid residue attached to a xylose residue other than the terminal non-reducing one. 5. Gel filtration of various xylanase fractions gave values for the molecular weight of the enzyme from 34000 to 38000.

Studies on the Activation Mechanism of Fibrinolytic Enzyme System in Plasma by Human Pancreatic Elastase

1982 ◽  
Vol 47 (01) ◽  
pp. 008-013 ◽  
Author(s):  
N Toki ◽  
S Takasugi ◽  
K Ishizu ◽  
H Sato ◽  
H Sumi
Keyword(s):  
Molecular Weight ◽  
Enzyme System ◽  
Fibrinolytic Enzyme ◽  
Activation Mechanism ◽  
Low Molecular Weight ◽  
Pancreatic Elastase ◽  
Α2 Macroglobulin ◽  
Plasmin Inhibitor

SummaryIn the present study, the activation mechanism of fibrinolytic enzyme system in plasma by human pancreatic elastase was investigated. It was confirmed that human pancreatic elastase not only converted the co-existing plasminogen to low molecular weight-plasminogen which could be easily activated by the activator, but also inhibited α2-macroglobulin and α2-plasmin inhibitor which are antiactivators or fast reacting antiplasmins, and consequently, induced the activation of the fibrinolytic enzyme system in plasma.

scholarly journals Thrombolytic properties of staphylokinase

Blood ◽  
1990 ◽  
Vol 76 (5) ◽  
pp. 925-929
Author(s):  
O Matsuo ◽  
K Okada ◽  
H Fukao ◽  
Y Tomioka ◽  
S Ueshima ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
Plasminogen Activator ◽  
The Other ◽  
Tissue Type ◽  
Plasminogen Activation ◽  
Plasma Clot ◽  
Tissue Type Plasminogen Activator ◽  
Other Hand ◽  
Type Plasminogen Activator

We evaluated the properties of recombinant staphylokinase in comparison with those of tissue-type plasminogen activator (t-PA) and streptokinase (SK). The presence of fibrin(ogen) fragment FCB-2 in the reaction mixture increased plasminogen activation by staphylokinase more than 20-fold. Such characteristics are similar to those of t-PA. On the other hand, SK was not affected by the presence of FCB-2. The thrombolytic properties of staphylokinase were studied in a system consisting of a radioactive human plasma clot (125I-fibrinogen-labeled) suspended in the circulating citrated plasma. Significant thrombolysis (50% in 3 hours) was obtained with 2 micrograms/mL of staphylokinase and 4.45 micrograms/mL t-PA, as compared with 12 micrograms/mL for SK. The relative molar potency of staphylokinase, calculated from the molecular weight, was about two times more effective than that of SK, but about half of that of t-PA. Systemic fibrinolytic activation and fibrinogen breakdown was not observed with staphylokinase or t-PA, but was observed with SK. The thrombolytic efficiency of staphylokinase, which was calculated as the ratio of the degree of thrombolysis/the degree of fibrinogenolysis, was about five times greater than that of SK, and about half of that of t-PA. These findings suggest that staphylokinase has higher specific thrombolytic properties and lesser fibrinogenolytic properties than those of SK.

scholarly journals Purification and some properties of a soluble benzene-oxidizing system from a strain of Pseudomonas

1975 ◽  
Vol 146 (1) ◽  
pp. 173-183 ◽  
Author(s):  
B C Axcell ◽  
P J Geary
Keyword(s):  
Molecular Weight ◽  
Carbon Source ◽  
Enzyme System ◽  
The Other ◽  
Benzene Oxidation ◽  
Soluble Enzyme ◽  
Iron Proteins ◽  
Protein Components ◽  
Haem Iron

1. A soluble enzyme system which oxidizes benzene to cis-1,2-dihydroxycyclohexa-3,5-diene (cis-benzene glycol) was obtained from a species of Pseudomonas grown on benzene as the major carbon source. 2. The system was shown to consist of three protein components. Two of these were non-haem-iron proteins of molecular weight approx. 21,000 and approx. 186,000 and the other was a flavoprotein of molecular weight approx. 60,000. 3. Fe2+ and NADH were essential cofactors for benzene oxidation.

MONOMER AND DIMER FORMS OF GAMMA-GLOBULIN POLYPEPTIDES IN NORMAL URINE

1964 ◽  
Vol 42 (12) ◽  
pp. 1815-1823 ◽  
Author(s):  
M. H. Freedman ◽  
G. E. Connell
Keyword(s):  
Molecular Weight ◽  
Disulfide Bonds ◽  
Gamma Globulin ◽  
The Other ◽  
Light Chains ◽  
Low Molecular Weight ◽  
Γ Globulins ◽  
Intermolecular Disulfide Bonds ◽  
Normal Urine ◽  
Polypeptide Chains

The γ-globulins of low molecular weight in human urine have been partially fractionated and characterized. The two principal components are made up of "light" polypeptide chains of 7 S γ-globulin. One of these components, the "monomer", has a molecular weight in dissociating solvents of approximately 20,000 and probably consists of single light chains. The other component, the "dimer", has a molecular weight of approximately 40,000 and probably consists of pairs of light chains joined by intermolecular disulfide bonds.

The similarity of histones from turtle erythrocytes and liver

1981 ◽  
Vol 59 (4) ◽  
pp. 273-279 ◽  
Author(s):  
R. G. Rutledge ◽  
C. E. Shay ◽  
G. L. Brown ◽  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Minor Component ◽  
Sea Turtle ◽  
Exchange Chromatography ◽  
The Other ◽  
Cation Exchange Chromatography ◽  
Mammalian Tissues ◽  
Exclusion Chromatography ◽  
A Minor ◽  
Molecular Exclusion Chromatography

Using the fresh-water "red-eared turtle" Pseudomys scriptans elegans, we have confirmed the existence of a minor component H1s among the lysine-rich histones of turtle erythrocytes by three forms of gel electrophoresis and two forms of chromatography. It was separated from the major components by both cation-exchange chromatography and molecular-exclusion chromatography and shown to differ slightly but significantly in content of several amino acids as well as being shorter than the other lysine-rich histones. Although its composition is close to that of the "tissue-specific" F1b of sea turtle erythrocytes, it is present in even greater relative amount in red-eared turtle livers. In most respects it resembles the satellite histone H10 of mammalian tissues. No unusual histones were observed among the perchloric acid insoluble histones of turtle erythrocytes.

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