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At least 1,189 records · Page 66Linked to original sources
PubMed1979

Valyl-tRNA synthetase from chick embryo brain. Properties of the sulfhydryl groups.

The number of thiol groups in valyl-tRNA synthetase [L-valine tRNA ligase (AMP) E.C.6.1.1.9] isolated from chick embryo brain was determined. Titration with 5.5'-dithiobis(2-nitrobenzoic) acid showed 11 free SH groups calculated on the basis of a molecular weight of 110000 daltons. In 8M urea reaction with DTNB revealed 1 additional SH-group. Binding of substrates to the active site of the molecule decreased the number of titratable SH-groups. The modification of enzyme activity was studied by the use of thiol reagents: metal ions Ag+, Cu2+, Hg2+ and pCMB. The ATP-PPi exchange activity of valyl-tRNA synthetase was significantly less inhibited by metal ions than the aminoacylation activity. SH-groups essential for tRNA acylation were not required for the activation of valine. After gamma irradiation of valyl-tRNA synthetase the number of SH-groups diminished parallel with the decrease in enzyme activity.

Amino Acyl-tRNA Synthetases↗
PubMed1983

Distributions of 35S-sulfate and 3H-glucosamine in the angular region of the hamster: light and electron microscopic autoradiography.

The distribution of 35S-sulfate and 3H-glucosamine in the angular region of the hamster was studied by light and electron microscopic autoradiography following intraperitoneal injection of these compounds to hamsters. Exposed silver grains of 35S-sulfate were concentrated in the trabecular meshwork, sclera, and cornea, and grains of 3H-glucosamine were localized in the trabecular region. The radioactivity of both isotopes was observed in the Golgi apparatuses of the endothelial cells of the angular aqueous plexus and the trabecular meshwork. The grains were noted over the entire cytoplasm, except for the nucleus, and then were incorporated into the amorphous substance and collagen fibers in the region adjacent to the angular aqueous sinus. These results suggest that endothelial cells in the angular region synthesize and secrete the sulfated glycosaminoglycans and hyaluronic acid.

Animals↗
PubMed1993

A simple chemical method for the oxidation of beta-hydroxybutyrate; application of the method for the estimation of ketone bodies.

A simple one-step method employing potassium persulphate as an oxidising agent in presence of catalyst, Ag2+, for the oxidation of beta-hydroxybutyrate (beta-OHB) to acetoacetate (AcAc) has been developed and standardized. Under the condition of assay, beta-OHB (0.079-0.395 microM) was quantitatively transformed to AcAc. The reaction linearity was observed from 0.079 to 0.634 microM. Optimum conditions were: pH, 6.2; temp., 40 degrees C; persulphate saturation, 40% and catalyst, 1.82 mM. Under the experimental condition, no reversal of inhibition caused by chloride (22.96 mM) was observed at Ag+ concentrations (9.09 and 18.18 mM), while higher conc. of Ag+ (27.27 mM) caused significant reversal of inhibition (about 60%). The maximum reversal of inhibition was achieved at Ag+ (36.36 mM). The level of ketone bodies, when estimated by the present method, was greatly enhanced during starvation period and about 2- and 12-fold higher level of ketone bodies was observed (compared to control) in rats fasted for 24 and 48 hr respectively.

3-Hydroxybutyric Acid↗