Search PubMed⌕ Search

Biomedical subjects

R Coleman

Publications and source records attributed to R Coleman.

At least 343 records · Page 19Linked to original sources
PubMed1976

The topographical location and unique nature of a glucokinase associated with the Golgi apparatus of rat liver.

A particulate glucokinase was recovered in the Golgi-rich fraction of rat liver prepared by the method of Morré [Methods Enzymol. (1971) 22, 130-148], thus extending the demonstration by Berthillier et al. [Biochim. Biophys. Acta (1973), 293, 370-378] of particulate glucokinase activity in a microsomal subfraction that showed enrichment in Golgi characteristics. The purity of this fraction was examined and it was then subjected to several treatments, the action of Triton X-100, freezing and thawing, and sonication to establish the topographical location of the glucokinase activity thus solubilized. The evidence suggests that the glucokinase activity is either soluble in the lumen of the Golgi apparatus or loosely associated with the inside of the Golgi membranes.

Animals↗
PubMed1975

The development and fine structure of ultimobranchial glands in larval anurans. II. Bufo viridis, Hyla arborea, and Rana ridibunda.

A comparative optical microscopic and ultrastructural study on the ultimobranchial (UB) glands of three common species of Israeli anurans: Bufo viridis, Hyla arborea, and Rana ridibunda during metamorphosis is presented. The UB glands typically consist of a single follicle with a central lumen, though occasionally secondary follicles are present in Hyla and Rana. A single UB cell type is found which appears either in a very electron-dense "dark" form or as a less dense "light" form, though the ratio of dark: light cells from gland to gland at any one stage of metamorphic development is quite variable. By the end of metamorphosis in Bufo and Hyla all the UB cells are usually of the light variety, whereas in Rana the dark cells persist. The organelles of these secretory cells including secretory granules, granular endoplasmic reticulum, free ribosomes, tonofilaments, microtubules, Golgi bodies, and lipid droplets, their distribution, abundance, and possible functions in relation to metamorphosis are described. Apocrine secretion into the central lumen of the gland is also described and discussed.

Amphibians↗
PubMed1975

Enzyme profiles of mammalian bile.

The activities of subcellular marker enzymes in bile and liver homogenate from several mammalian species have provided information on the specificity of protein release during bile formation. The presence of significant amounts of the plasma membrane enzymes alkaline phosphodiesterase I and leucyl-beta-naphthylamidase in bile, in addition to alkaline phosphatase and 5'-nucleotidase, and the relative absence of intracellular enzymes lends support to the view that bile salt liberation from the hepatocyte is accompanied by a partial solubilization of the plasma (canalicular) membrane without extensive damage to the whole hepatocyte.

Alkaline Phosphatase↗
PubMed1975

Hydrolysis of erythrocyte membrane phospholipids by a preparation of phospholipase C from Clostridium Welchii. Deactivation of (Ca-2+, Mg-2+)-ATPase and its reactivation by added lipids.

1. Haemoglobin-free erythrocyte ghosts were prepared in 40 imosM bicarbonate buffer, pH 7.4, containing 1 mM EDTA (40 imosM/l mM EDTA). The ghost preparation was highly permeable on preparation but partially resealed on incubation in media containing Ca-2+. 2. A partially purified preparation of phospholipase C from Clostridum welchii caused an increase in observed Mg-2+-ATPase activity, reflecting a change in the permeability of the ghost to substrate. The phospholipase did not decrease Mg-2+-ATPase even at the highest levels tested. Mg-2+-ATPase activity could therefore be used as a permeability indicatior in these experiments. 3. Both (Ca-2+, Mg-2+)-ATPase activities of the ghosts were progressively lost as a result of the phospholipid hydrolysis induced by phospholipase C. 4. When a haemolysin in the commercial preparation was destroyed by heat-treatment, deactivation of the (Ca-2+, Mg-2+)-ATPase and (Na+, K+, Mg-2+)-ATPases were still observed but permeability changes were greatly reduced. 5. The products of phospholipase action were not inhibitory to the Ca-2+, Mg-2+)-ATPase. 6. Lysolecithin brought about a reactivation of the (Ca-2+, Mg-2+)-ATPase which was superimposed upon permeability changes in the preparation. 7. Reactivation of the (Ca-2+, Mg-2+)-ATPase was brought about by a nonlytic, mixed lipid preparation without significant effect upon permeability. 8. Human erythrocyte (Ca-2+, Mg-2+)-ATPase therefore appears to be an enzyme which responds to perturbation of the lipid environment in the membrane and is a "lipid-dependant" enzyme.

Adenosine Triphosphatases↗
PubMed1975

Basolateral plasma membranes of intestinal epithelial cells. Identification by lactoperoxidase-catalysed iodination and isolation after density perturbation with digitonin.

Lactoperoxidase-catalysed iodination was used to label intestinal epithelial cell sheets with 125I. The iodination was carried out under conditions that allowed little penetration of lactoperoxidase into the cells and membrane-bound 125I therefore provided an effective marker for following plasma-membrane fragments through subcellular-fractionation procedures. 2. After homogenization and isopycnic zonal centrifugation through sucrose gradients two peaks of membrane-bound 125I were detected. One coincided with brush border enzymes such as alkaline phosphatase, disaccharidases and L-leucine B-naphthylamidase, whereas the other was coincident with the major peak of (Na++K+)-stimulated ATPase (adenosine triphosphatase), which has been thought to be concentrated in the basolateral plasma membranes of these cells. Neither peak of 125I reflected the distribution of any marker for an intracellular organelle. 3. A larger proportion of the (Na++K+)-stimulated ATPase, and thus of the basolateral plasma-membrane material, was found in a crude 'mitochondrial' fraction. It was not readiily separated from mitochondria by conventional techniques of subcellular fractionation. 4. Treatment of the 'mitochondrial' fraction with digitonin increased the density of basolateral plasma membrane but had little effect on mitochondrial density. A purified preparation of digitonin-loaded basolateral plasma membranes was isolated at a density of 1.20-1.22 by isopycnic centrifugation. 5. The enzymic composition of this preparation of basolateral plasma membranes is compared with previous preparations isolated from intestinal mucosal 'scrape' materials and from isolated cells.

Adenosine Triphosphatases↗