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Biomedical subjects

M Matsuo

Publications and source records attributed to M Matsuo.

At least 577 records · Page 32Linked to original sources
PubMed1977

Immunological stability in vitro and in vivo of eel calcitonin.

The immunological activity of eel calcitonin was more persistent than that of porcine and human calcitonin when incubated in vitro with rabbit serum, human serum, liver homogenate or kidney homogenate, respectively. Both eel and human calcitonin were more stable than porcine calcitonin when injected iv into rabbits.

Animals↗
PubMed1977

Stability of [Asu1,7]-eel calcitonin and eel calcitonin in vitro and in vivo.

Stability of [Asu1,7]-eel calcitonin was compared with that of eel calcitonin by the radioimmunoassay method. [Asu1,7]-Eel calcitonin cross-reacted with anti-eel calcitonin antisera. [Asu1,7]-Eel calcitonin was as stable as eel calcitonin in rabbit liver or rabbit kidney extracts when incubated at 37 degrees C. Disappearance curves from the plasma of [Asu1,7]-eel calcitonin and eel calcitonin following iv injection in rabbits were quite similar.

Animals↗
PubMed1977

The enhancement of phagocytosis and intra-cellular killing of Pseudomonas aeruginosa and its common antigen (OEP) coated latex particles by mouse spleen macrophages to which anti-OEP-IgG and gentamicin have been added.

This experiment was performed using macrophages derived from mouse spleens immunized or non-immunized with the common antigen (OEP) of Pseudomonas aeruginosa. The phagocytosis of these macrophages of live or formalin killed Pseudomonas aeruginosa and latex particles coated with OEP were enhanced by the addition of anti-OEP-IgG, but not by immunoglobulin taken from normal mice. The macrophages from mice immunized with OEP showed significantly enhanced phagocytosis of latex particles coated with OEP, but not of live or killed bacteria. The effects of anti-OEP-IgG and gentamicin on phagocytosis and intracellular killing were compared in cases where only anti-OEP-IgG or only getamicin were used as well as in cases where the two were combined. It was found that the two combined was far more effective on phagocytosis and intracellular killing. Furthermore, there was little or no difference in the results depending on whether macrophages from mice immunized or non-immunized with OEP were used.

Animals↗
PubMed1976

Partial purification and characterization of a triglyceride lipase from pig adipose tissue.

A triglyceride lipase was extracted from defatted pig adipose tissue powder with dilute ammonia and purified about 230-fold by a combination of ammonium sulfate fractionation, heparin-Sepharose 4B, DEAE-cellulose, and Sephadex G-150 column chromatographies and isoelectrofocusing electrophoresis. The enzyme was distinguishable in physical and kinetic properties from the two previously defined lipases in adipose tissue, lipoprotein lipase, and hormone-sensitive lipase. The purified enzyme was fully active in the absence of serum lipoprotein and was not stimulated by adenosine 3':5'-monophosphate-dependent protein kinase. In marked contrast to the already defined lipases, the enzyme was strongly inhibited by serum albumin. The enzyme had a molecular weigt of about 43,000, a pI of 5.2, and pH optimum of 7.0. The enzyme hydrolyzed triolein to oleic acid and glycerol, and did not exhibit esterase activity. The apparent Km for triolein was 0.05 mM. Physiological roles of this new species of lipase remained to be explored.

Adipose Tissue↗
PubMed1976

A radical scavenging reaction of alpha-tocopherol with methyl radical.

To study a radical scavenging reaction of alpha-tocopherol, it was reacted with methyl radical in dimethyl sulfoxide. Two main products, a geminal dimethyl cyclohexadienone and methyl ether of alpha-tocopherol, were obtained and these structures were determined by 13C nuclear magnetic resonance spectroscopy. The radical methylation data of alpha-tocopherol suggested that a delocalize radical species would be an intermediate.

Chemical Phenomena↗
PubMed1976

Studies on triglyceride lipases from rat adipose tissue.

A new assay procedure for triglyceride lipase [EC 3.1.1.3] was developed in which radioactive triolein was dissolved in ethanol and directly added to the reaction mixture in the absence of serum and albumin. In the rat adipose tissue there appeared to be a triglyceride lipase measurable with this assay in addition to the two previously defined lipases, lipoprotein lipase [EC 3.1.1.34] and hormone-sensitive lipase. The enzyme was active in the absence of serum and was strongly inhibited by albumin. The molecular weight was estimated to be about 42,000. Adenosine 3',5'-monophosphate-dependent protein kinase [EC 2.7.1.27] was unable to activate the enzyme. The three species of lipases mentioned above behaved differently upon chromatography on a Sepharose 4B column, and were distinguishable from each other in their physical and kinetic properties. The physiological roles of the new species of lipase remain to be explored.

Adipose Tissue↗