scholarly journals Biophysical Interpretation on the Biological Actions of Radiations (I) (Correspondence between the Relay-contact System and the Gene-enzyme System and Some Discussions on the Target Theory)

1961 ◽  
Vol 2 (1) ◽  
pp. 42-60
Author(s):  
Yasushi NISHIWAKI
Keyword(s):  
Enzyme System ◽  
Contact System ◽  
Relay Contact ◽  
Target Theory ◽  
Biological Actions

Electron Microscopic and Isozyme Study of a Case of Ochronosis

1972 ◽  
Vol 30 ◽  
pp. 88-89
Author(s):  
Jay W. Cha ◽  
Perry J. Melnick
Keyword(s):  
Benzene Ring ◽  
Enzyme System ◽  
Homogentisic Acid ◽  
Degenerative Changes ◽  
Acid Oxidase ◽  
Electron Microscopic ◽  
Tyrosine Metabolism ◽  
Collagenous Tissues

Hereditary ochronosis in very few cases has been examined electron microscopically or histochemically. In this disease homogentisic acid, a normal intermediary of tyrosine metabolism, forms in excessive amounts. This is believed to be due to absence or defective activity of homogentisic acid oxidase, an enzyme system necessary to break the benzene ring and to further break it down to fumaric and acetoacetic acids. Ochronotic pigment, a polymerized form of homogentisic acid, deposits mainly in mesenchymal tissues. There has been a question whether the pigment originates from the collagenous tissues, or deposits passively, where in contrast to melanin it induces degenerative changes.

Plasma Prekallikrein Activity in Patients with Total Hip Arthroplasty

1987 ◽  
Vol 58 (04) ◽  
pp. 1040-1042
Author(s):  
J J M L Hoffmann ◽  
J H J P M Kortmann
Keyword(s):  
Total Hip Arthroplasty ◽  
Hip Arthroplasty ◽  
Hip Prosthesis ◽  
Contact System ◽  
Factor Xii ◽  
Total Hip ◽  
Activity Factor ◽  
Patient Groups ◽  
Kallikrein Activity

SummaryThe behaviour of the contact system was studied in 40 patients with total hip arthroplasty, by measuring plasma prekallikrein, spontaneous kallikrein activity and factor XII. In the literature it had been shown that patients with complications from this operation had decreased prekallikrein and increased kallikrein activity (M. Nakahara. Acta orthop scand 1982; 53: 591-6). In the present study, comprising patients with and without pain and proven loosening of the hip prosthesis, these findings could only partially be confirmed. Patients with a loosened prosthesis had significantly lower prekallikrein (mean 0.78 ± 0.28 U/ml; p <0.01) than patients without problems, but no detectable kallikrein activity in plasma. Patients with pain but no loosening had normal prekallikrein (1.04 ±0 0.26 U/ml) and also no demonstrable kallikrein activity. Factor XII was normal in all patient groups. It is concluded that decreased prekallikrein is limited to patients with a loosened hip prosthesis, with or without pain.

Western Blot Analyses of Prekallikrein and its Activation Products in Human Plasma

1991 ◽  
Vol 65 (04) ◽  
pp. 382-388 ◽  
Author(s):  
Dulce Veloso ◽  
Robert W Colman
Keyword(s):  
Complex Formation ◽  
Western Blot ◽  
Human Plasma ◽  
Contact System ◽  
Plasma Activation ◽  
Normal Plasma ◽  
Sds Page ◽  
Activation Products ◽  
Major Antigen ◽  
Formation Of Complexes

SummaryPrekallikrein (PK), a zymogen of the contact system, and its activation products, kallikrein (KAL), KAl-inhibitor complexes and fragments containing KAL epitope(s) have been detected in human plasma by immunoblotting with a monoclonal anti-human plasma PK antibody, MAb 13G1L. Detection of antigen-MAb 13G11 complexes with peroxidase-conjugated anti-IgG showed that the two variants of PK (85- and 88-kDa) are the only major antigen species in normal, non-activated plasma. Upon plasma activation with kaolin, the intensity of the PK bands decreased with formation of complexes of KAL with CL inhibitor (C1 INH) and α2-rrtzcroglobulin (α2M) identical to those formed by the purified proteins. Immunoblots of normal plasma showed good correlation between the PK detected and the amount of plasma assayed. Increasing amounts of KAL incubated with a constant volume of PK-deficient plasma showed increasing amounts of KAL and of KAL-C1 INH and KAL-α2M complexes. Complexes of KALantithrombin III (ATIII) and the ratio of KALα2M/ KAL-CL INH were higher in activated CL INH-deficient plasmas than in activated normal plasmas. Protein resolution by 3-12% gradient SDS-PAGE and epitope detection with [125I]MAb 13G11 showed four KALα2M species and a 45-kDa fragment(s) in both surface-activated normal plasma and complexes formed by purified KAL and α2M. Immunoblots of activated plasma also showed bands at the position of KALCL INH and KALATIII complexes. When α1-antitrypsin Pittsburgh (cα1-AT, Pitts) was added to plasma before activation, KAL-α1-ALPitts was the main complex. The non-activated normal plasma revealed only an overloaded PK band. This is the first report of an antibody that recognizes KAL epitope(s) in KAL-α2M, KALATIII and KALa1-α1Pitts complexes and in the 45-kDa fragment(s). Therefore, MAb 13G11 should be useful for studying the structure of these complexes as well as the mechanism of complex formation. In addition, immunoblotting with MAb 13G11 would allow detection of KAl-inhibitor complexes in patient plasmas as indicators of activation of the contact system.

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.

Kinetic Aspects of the Interaction of Blood Clotting Enzymes

1965 ◽  
Vol 13 (01) ◽  
pp. 155-175 ◽  
Author(s):  
H. C Hemker ◽  
P.W Hemker ◽  
E. A Loeliger
Keyword(s):  
Kinetic Analysis ◽  
Enzyme Kinetics ◽  
Blood Clotting ◽  
Enzyme System ◽  
Enzyme Kinetic ◽  
Clotting Time ◽  
Standard Methods

SummaryApplication of the methods of enzyme-kinetic analysis to the results of clotting tests is feasible and can yield useful results. However, the standard methods of enzyme kinetics are not applicable without modifications imposed by the peculiarities of the blood-clotting enzyme system. The influence of the following complicating circumstances is calculated :1. Substrate is not present in excess.2. Only relative measures exist for concentrations of substrate or enzymes.3. Enzymes and substrates are often added together.4. Reagents are not pure.5. Clotting-time is our only measure for clotting-velocity.Formulas are deduced, which makes it possible to recognize the effect of these complications.

EVALUATION OF ERRORS OF THE FIRST AND SECOND ORDER DETERMINING THE SPEED OF A MOVING CONTACT SYSTEM GAS INSULATED SWITCH

2017 ◽  
Vol 2017 (48) ◽  
pp. 110-114
Author(s):  
V.M. Kutin ◽  
◽  
O.E. Rubanenko ◽  
S.V. Mysenko ◽  
◽  
...  
Keyword(s):  
Second Order ◽  
Contact System ◽  
Moving Contact

Kinin-Forming Enzyme System in DIC

1979 ◽  
Vol 10 (1) ◽  
pp. 98-101
Author(s):  
Masahiro MAKI ◽  
Kenji SOGA
Keyword(s):  
Enzyme System
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