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Biomedical subjects

S Kume

Publications and source records attributed to S Kume.

At least 145 records · Page 8Linked to original sources
PubMed1982

Correlation of the level of beta-citryl-L-glutamic acid with spermatogenesis in rat testes.

beta-Citryl-L-glutamic acid, which is known to be highly concentrated in the brains of immature animals, is preferentially localized in the testes of various adult animals, including mammals, amphibians and fish, mainly in the germinal cells. In young rats, the citrylglutamate concentration increases with age and coincides with the development of late spermatocytes into early spermatids. Rats with seminiferous tubule failure induced by ductuli efferentes ligation and experimental cryptorchidism are infertile as a result of germ cell depletion, especially spermatocytes and early spermatids. In these animals, the testicular citrylglutamate content was much lower than in normal testes.

Animals↗
PubMed1977

A specific method for the determination of threonine in rat blood plasma using aldehyde dehydrogenase.

A simple and sensitive method for the determination of threonine in rat blood plasma using aldehyde dehydrogenase after oxidation with periodate was developed. By the present method, threonine could be completely discriminated from serine and determined at the nanomole level. The amount of threonine in rat blood plasma obtained by the present method coincided well with the value determined on an amino acid analyzer.

Aldehyde Oxidoreductases↗
PubMed1975

Synthesis of adenosine triphosphate by way of potassium-sensitive phosphoenzyme of sodium, potassium adenosine triphosphatase.

The sodium and potassium ion pump is an intrinsic enzyme of plasma membranes. In these experiments it was driven backward in a transient two-step operation involving, first, phosphorylation of the enzyme from inorganic phosphate, and second, transfer of the phosphate group from the enzyme to ADP upon addition of a high concentration of Na+. There was no evidence of a significant concentration gradient across the membranes. Na+ presumably reached the solutions on both faces of the membrane simultaneously and provided the energy for synthesis simply as a consequence of ligand binding. An interaction free energy between the free energy of the binding of Na+ and the free energy of hydrolysis of the phosphate group on the enzyme was estimated. The experiments also suggested a feature of the transport mechanism. This is control by phosphorylation of access pathways from the solutions in contact with the faces of the membrane to an active center for cation binding. In the dephosphoenzyme access would be to the intracellular solution and in the phosphoenzyme access would be to the extracellular solution.

Adenosine Diphosphate↗