Showing papers by "Hiroshi Yoshida published in 1968"
TL;DR: The iodination of a certain number of minor nucleosides shows that the derivatives of uridine having C-5–C-6 double bond can react, whereas dihydrouridine remains intact.
9 citations
TL;DR: In order to clarify the mechanism of cation and water transport in the subcellular level of kidney, it is necessary to clearly demonstrate the fine structural localization of Na-K-ATPase activity by histochemical method.
Abstract: There is evidence that ATPase plays a contributory role in providing energy for the active transport of cations across the cellular membranes of kidney (C harnoc k, and Post, 1963, K insol v in g, et al., 1963), brain (S k o u, 1960) and muscle (S c h w art z, and Laester, 1964). S k o u (1960) and Post et al. (1960) discussed in detail the relationship of the cation transport and Na-K-ATPase (EC 3, 6, 1, 3) which was activated by sodium in the presence of magnesium and potassium and inhibited by certain cardiac glycosides. Generally, W a c h s t e i n-M e i s e l's (1957) method for histochemistry has been used by many workers for the electron microscopic demonstration of ATPase (R o s t g a a r e, and B e h n e k, 1965, Peter, and Nakao, 1966). However, addition of sodium, potassium and calcium or ouabain to media used in conventional methods does not influence enzyme activity (B o n t i n g, et al., 1962, No v i k of f et al., 1961). In order to clarify the mechanism of cation and water transport in the subcellular level of kidney, it is necessary to clearly demonstrate the fine structural localization of Na-K-ATPase activity by histochemical method. We have attempted to study the localization of Na-K-A TPase and K-dependent neutral phosphatase which may have a correlation with Na-K-ATPase, by approximate assay system used in the biochemical study of enzymes. In this study, histochemical and
2 citations