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K Oshima

Publications and source records attributed to K Oshima.

At least 235 records · Page 13Linked to original sources
PubMed1981

Kallikrein concentrations in the plasma, lymph, thoracic, and cerebrospinal fluid of rabbits.

Since there is not an established method for selective assay of kallikrein, it is still unsettled whether kallikrein is absorbed from the intestine or not. Kallikrein was injected into the duodenum of rabbits which had been fasted for 24 hr and the concentrations of the drug in the plasma, lymph and cerebrospinal fluid were determined by an enzymatic method using substrate TAME or Peptide-MCA (hereafter, briefly as TAME method or Peptide-MCA method). An unknown substance, which splits the substrate TAME, appeared in the plasma, lymph and cerebrospinal fluid after injection of kallikrein into the rabbit duodenum. In rabbits which underwent pancreatectomy, kallikrein was not absorbed from the intestine and the unknown substance was not detected in any of the plasma, lymph and cerebrospinal fluid.

Animals↗
PubMed1980

The presence of progesterone receptors in the sexual skin of the monkey.

R5020(17,21-dimethyl-19-nor-4,9-pregnadiene-3,20-dione)-binding components with sedimentation coefficient of 8S were detected in sexual skin cytosols from estrogen-primed ovariectomized Japanese monkey (Macaca fuscata fuscata). In contrast, little 8S binding was found in similar preparations from the abdominal skin. The dissociation constants and the number of binding sites of the components were 1.6 x 10(-10)M and 36 fmoles/mg cytosol protein, respectively. The 8S binding components were specific for progestational compounds. Incubation with pronase abolished the 8S binding. Thermal experiments revealed the thermolabile nature of the components. Moreover, the concentration of the R5020-binding components was markedly increased by estradiol-17 beta 3-benzoate injections. We conclude from these results that the cytosols from the sexual skin of estrogen-primed female monkeys contain progesterone receptors.

Animals↗
PubMed1980

Isolation and characterization of aminotripeptidase from monkey brain.

Aminotripeptidase [EC 3.4.11.4] was purified from monkey brain by a five-step procedure comprising extraction from brain homogenate, ammonium sulfate fractionation, DEAE-cellulose chromatography, hydroxylapatide chromatography, and Sephadex G-200 gel filtration. A purification of 1,100-fold over the homogenate was achieved and the yield was 12%. The purified enzyme appeared to be homogeneous on polyacrylamide gel electrophoresis at pH 8.9. The amino acid composition of the enzyme resembled that of the pig kidney enzyme. The molecular weight of the enzyme was estimated to be about 65,000 by gel filtration on Sephadex G-200 and 70,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The pH optimum for L-leucyl-glycyl-glycine was about pH 7.5. The enzyme hydrolyzed only tripeptides to yield the NH2-terminal residues as free amino acids and the residual dipeptides. The enzyme did not show activities of arylamidase or carboxypeptidases A and B. The enzyme was inhibited by PCMB, o-phenanthroline, and bestatin. The inhibition by bestatin was competitive and the K1 value was calculated to be 5 X 10(-7) M.

Amino Acids↗