Biomedical subjects

Y Suketa

Publications and source records attributed to Y Suketa.

63 records · Page 4Linked to original sources

PubMed1976

Changes of ion mobilizations and their related enzyme activities in the blood of fluoride-intoxicated rats.

Fluoride concentrations in plasma 3 hr after a single oral dose of NaF (5 mg/100 g body weight) were increased 26 times above the control, but the concentrations in erythrocytes and red cell membranes were increased only 1.8 and 1.5 times over the respective control levels. Ionic concentrations of magnesium and calcium in erythrocytes and their membranes were significantly changed by fluoride administration, but the ionic concentrations in plasma were not statistically changed in comparison with controls. Acid phosphatase activities in plasma and erythrocytes were significantly decreased by fluoride administration, but alkaline phosphatase activity in the plasma was not changed. Mg2+-activated ATPase activity was significantly elevated in the erythrocyte membrane by fluoride administration; (Na+ + K+)-activated ATPase activity was significantly decreased in the membrane.

Acid Phosphatase↗

PubMed1975

Active site directed inactivators of mouse submaxillary renin.

The following active site directed inactivators for the pressor enzyme renin were synthesized: L-alpha-bromo-isocaproyl(BIC)-Leu-Val-Tyr-Ser-OH, L-BIC-Val-Tyr-Ser-OH, L-BIC-Leu-Val-OCH3, L-BIC-Leu-Val-OH, L-BIC-Val-Tyr-NH2, L-BIC-Val-Tyr-OCH3, L-BIC-Val-Tyr-OH, L-BIC-Leu-OCH3, L-BIC-Val-OCH3, and L-BIC-OCH3. The rate of inactivation of mouse submaxillary gland renin by these reagents was studied under a variety of conditions. L-alpha-Bromoisocaproyl-Val-Tyr-Ser-OH and L-alpha-bromoisocaproyl-Leu-Val-Tyr-Ser-OH and L-alpha-bromoisocaproyl-Leu-Val-Tyr-Ser-OH were the most efficient inactivators followed by L-alpha-bromoisocaproyl-Val-Tyr-NH2. The rates of inactivation by the first two peptides were strongly dependent on pH, being most efficient at low pH, least efficient at pH near 5.6, and becoming efficient again at neutral pH. The rate of the inactivation by L-alpha-bromoisocaproyl-Val-Tyr-NH2, in which the C-terminal carboxyl group is blocked, was only slightly dependent on pH. Complete inactivation was achieved by these three reagents. The inactivation was accompanied by incorporation of a stoichiometric quantity of the radiolabeled reagents. Based on these findings it was concluded that the inactivators reacted with a carboxyl group(s) in the active site of the renin molecule to form an esteric linkage. These data also suggest that a carcoxyl group(s) may constitute part of the catalytically essential functional groups in renin action. D-alpha-Bromoisocaproyl derivatives of the various peptides mentioned above were also prepared. These compounds were much less active than the L isomers indicating that the inactivation by the L-alpha-bromoisocaproyl peptides was a specific reaction.

Journal Article↗

PubMed1975