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Biomedical subjects

M Nakashima

Publications and source records attributed to M Nakashima.

At least 595 records · Page 33Linked to original sources
PubMed1977

Glass electrode measurement of net Na+ and K+ fluxes in erythrocytes of the spontaneously hypertensive rat.

The exchange of Na+ and K+ in rat red cells at 40% hematocrit incubated in a physiological salt solution containing 1 MM ouabain was monitored with ion-specific glass electrodes. Because this system measures a change in the activity of an ion as a logarithmic function of its preexisting level, delta[K+]o is more accurately measured than delta[Na+]o; within this limitation, the downhill ion movements were close to 1:1 over the temperature span from 37 to 3 degrees C. These transmembrane movements are reasonably well expressed in terms of first-order kinetics and an Arrhenius plot constructed for K+ as the accurate indicator of the exchange yields an activation energy of 12 kcal/mol. A well-defined reversal of the usual direct relation of temperature to exchange rate was observed between 6 and 3 degrees C. The net ion movements were distinctly faster at low temperature in cells from rats with spontaneous hypertension (SHR-Okamoto) than in cells from matched controls (Woodlyn and WKY).

Animals↗
PubMed1976

Increased erythrocyte permeability to Li and Na in the spontaneously hypertensive rat.

Red blood cells incubated in a physiological medium in which Li replaces Na (LiPSS) gain Li in exchange for Na and K. The rate of Li uptake is modestly but significantly increased in the spontaneously hypertensive rat (SHR) at 37 degrees C and at 22 degrees C. The slow rate of Na gain and K loss during cooling at 2 degrees C was about doubled in unmodified whole blood samples from the SHR.

Animals↗
PubMed1975

Protamine kinase from yeast.

A protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37) which preferentially phosphorylates protamine is purified about 250-fold from the soluble fraction of baker's yeast (Saccharomyces cerevisiae). This enzyme is not sensitive to activation by cyclic nucleotides. Histone is about 5% as active as protamine in the reaction rate. Neither casein, phosvitin nor glycogen phosphorylase is active as substrate. The enzyme is distinguishable from casein kinase of the classical type (Rabinowitz, M. and Lipmann, F. (1960) J. Biol. Chem. 235, 1043-1050) and from adenoshine 3', 5'-monophosphate-dependent protein kinase described earlier (Takai, Y., Yamamura, H. and Nishizuka, Y. (1974) J. Biol. Chem. 249,530-535).

Caseins↗
PubMed1975

Cell Na and K in the rat tail artery during the development of hypertension induced by desoxycorticosterone acetate.

An increase in total Na, due in large part to an increase in cell Na, was measured in the freshly excised rat tail artery during the course of DOCA-saline treatment. Since this change was associated with a fall in cell K, was first observed at 2 weeks, coincident with the rise in blood pressure, and was not sustained during subsequent immersion of the artery at zero pressure, it probably reflects the high in vivo intravascular pressure. In the incubated artery, cell Na is significantly reduced early in the course of treatment, while cell K falls late. Thus, Na transport in the artery is under direct attack from the start, but it is suggested that this leads to hypertrophy rather than to vasoconstriction.

Animals↗