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Biomedical subjects

Y Takada

Publications and source records attributed to Y Takada.

At least 667 records · Page 37Linked to original sources
PubMed1983

The activation of two isozymes of glu-plasminogen (I and II) by urokinase and streptokinase.

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.

Electrophoresis, Polyacrylamide Gel↗
PubMed1983

The degradation of urate in liver peroxisomes. Association of allantoinase with allantoicase in amphibian liver but not in fish and invertebrate liver.

Allantoinase and allantoicase were co-purified from frog (Rana catesbeiana) liver. The ratio of the two enzyme activities remained constant during purification and was unchanged by a variety of treatments of the purified enzyme. These results suggest that allantoinase and allantoicase are located in the same protein. It was found that the two hepatic enzyme activities are also associated with the same protein in other frogs (Xenopus laevis and Rana nigromacultata), tadpoles (R. catesbeiana), and newts (Triturus pyrrhogaster). In contrast, allantoinase and allantoicase were found to be different proteins in marine fish and invertebrate liver.

Amidohydrolases↗
PubMed1983

Localization of human seminal plasma No. 7 antigen (Ferrisplan) in accessory glands of male genital tract and spermatozoa.

The establishment of a hybridoma (1C4) producing sperm immobilizing monoclonal antibody to human seminal plasma No. 7 antigen (HSP No. 7 Ag.) and the isolation of the pure antigen by immunoaffinity chromatography bound monoclonal antibodies have been reported previously. In the present investigation, HSP No. 7 Ag. has been termed 'Ferrisplan' and its distribution in male genital organs, spermatozoa and body fluids has been studied. The amount of Ferrisplan in the body fluids was determined by radioimmunoassay. Large amounts were detected in seminal plasma and milk, trace amounts in saliva, and none in the serum and urine. The concentration of Ferrisplan was highest in the seminal plasma of azoospermic patients and gradually decreased from oligospermia to normospermia. Using an immunofluorescent method with anti-Ferrisplan monoclonal antibody, strong staining was observed on the epithelial layers of human seminal vesicles, no staining on testes and bright staining on the post-nuclear cap and mid-piece segment of spermatozoa. These results indicate that Ferrisplan is excreted mainly from the seminal vesicle and adheres to the post-nuclear cap and mid-piece of the spermatozoa as a sperm-coating antigen.

Antigens↗
PubMed1983

Characterization and immunohistologic demonstration of angiotensin-converting enzyme in human renal cell carcinoma.

Angiotensin-converting enzyme (ACE, EC 3.4.15.1) was demonstrated in the tissue of human renal cell carcinoma and its cultured cells by immunofluorescence and immunohistochemistry using a specific rabbit antibody to human kidney ACE. The biochemical properties of the partially purified enzyme from the tumor tissue were identical with the pure enzyme from normal kidney with respect to Km, optimal pH, chloride ion activation and heat sensitivity. Catalytic activities of tumor and normal kidney enzymes were similarly inhibited by an ACE inhibitor, captopril, and by the antibody to human kidney ACE. However, double immunodiffusion analysis showed spur-forming immunoprecipitin bands between the tumor and normal kidney enzyme. These data suggest that human renal cell carcinomas have a new isozyme of ACE differing in part immunologically from the enzyme of normal kidney.

Adenocarcinoma↗
PubMed1983

[Experimental and clinical studies on latamoxef in the perinatal period].

Pharmacokinetics and clinical studies on the perinatal use of latamoxef (LMOX, Shiomarin), a new parenteral oxacephem antibiotic, were carried out and the results obtained were as follows: After LMOX was intravenously given to mother at a dose of 1 g, the umbilical cord serum concentration of LMOX reached to peak with 18.4 micrograms/ml in 1 hour 20 minutes and its concentration was higher than the maternal serum after 2 hours 25 minutes and decreased gradually (T 1/2 beta = 1.61 hours). The materno-fetal transfer of LMOX was 71.0%. LMOX showed the good transfer as well as other cephalosporins. After LMOX was intravenously administered to mother at a dose of 1 g, LMOX concentration in milk wasn't detectable up to 12 hours. LMOX was intravenously administered to 18 cases with premature rupture of membrane, at a daily dose of 2 g for 3--6 days. The prophylactic effects were observed in all cases, both mother and neonate. No adverse effects were observed in mother except for 1 case with low grade abnormality of S-GPT, transiently. We observed 3 neonates with jaundice (total bilirubin greater than or equal to 17.0 mg/dl) probably not related to LMOX. It is concluded that LMOX is less toxic, safe and clinically useful antibiotic for the treatment of perinatal infections.

Bacterial Infections↗
PubMed1982

Reversible depression of spontaneous brain electrical activity induced by actinomycin D and 7-aminoactinomycin D in rats.

Various types of actinomycin (C,D,S2, I and V) and 7-amino-analogue of actinomycin D were injected into the right lateral ventricle of the brain through a chronically implanted cannula. In rats but not in mice actinomycin D, actinomycin S2 and 7-aminoactinomycin D caused depression of EEG, while cardiac and respiratory activity were maintained. This effect of the EEG was reversible and a normal EEG pattern reappeared at least 3 h after administration.

Animals↗
PubMed1982

Activation pathway of glu-plasminogen to Lys-plasmin by urokinase.

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.

Electrophoresis, Polyacrylamide Gel↗
PubMed1982

Potentiation of the activation of Glu-plasminogen by streptokinase and urokinase in the presence of fibrinogen degradation products.

When Glu-plasminogen was activated by streptokinase (SK), the presence of early degradation products of fibrinogen (FgDP) enhanced the rate of activation. When various fragments of FgDP were fractionated, FgDP-Y and E fragments had a potentiating activity while D fragment did not. When Glu-plasminogen was activated by urokinase (UK), the activation rate was enhanced by every fragment of FgDPs, i.e. X, Y, D and E. Although both D and E fragments seem to be able to bind with lysine binding sites of Glu-plasminogen, and to enhance the activation rate by UK, only binding of E fragment with plasminogen can result in enhancement of the activation of Glu-plasminogen by SK.

Drug Synergism↗
PubMed1982

Biochemical and immunological studies of angiotensin converting enzymes from human, bovine, dog, hog, rabbit, rat and sheep kidneys.

1. Molecular and kinetic properties of angiotensin converting enzymes from seven different species' kidneys were similar concerning apparent molecular weight, heat sensitivity, Km value, optimum pH, activation by chloride ion, and inhibition by specific converting enzyme inhibitors (captopril and SA 446). 2. Rabbit antibody against pure human kidney enzyme cross-reacted partially with each animal kidney enzyme except for the rabbit enzyme. Antigenic determinants of animal enzymes were variable from species to species and differed from those of the human enzyme in extent and specificity.

Angiotensin-Converting Enzyme Inhibitors↗
PubMed1982

Subcellular distribution, and physical and immunological properties of hepatic alanine: glyoxylate aminotransferase isoenzymes in different mammalian species.

1. Subcellular distribution, and physical and immunological properties of hepatic alanine: glyoxylate aminotransferase isoenzymes 1 and 2 were examined with ten different mammalian species. 2. Intracellular organelles containing isoenzyme 1 varied from species to species; isoenzyme 1 was located in the peroxisomes, mitochondria or both organelles. In contrast, isoenzyme 2 was found only in the mitochondria but not in the peroxisomes. 3. In any species, isoenzyme 1 had molecular weight of approx. 80,000 with two identical subunits, and isoenzyme 2 approx. 200,000 with four identical subunits. 4. In any species, an immunological cross-reactivity was observed among isoenzymes 1 and among isoenzymes 2 but did not between isoenzymes 1 and isoenzymes 2.

Alanine Transaminase↗