Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Cysteic Acid”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 55 records · Page 3Linked to original sources
PubMed1982

Purification and characterization of cysteic acid and cysteine sulfinic acid decarboxylase and L-glutamate decarboxylase from bovine brain.

L-Cysteic and cysteine sulfinic acids decarboxylase (CADCase/CSADCase) and L-glutamic acid decarboxylase (GADCase), the synthetic enzymes for taurine and gamma-aminobutyric acid, respectively, have been purified to homogeneity from bovine brain. Although CADCase/CSADCase and GADCase copurified through various column procedures, these two enzymes can be clearly separated by a hydroxyapatite column. The purification procedures involve ammonium sulfate fractionation, column chromatographies on Sephadex G-200, hydroxyapatite, DEAE-cellulose, and preparative polyacrylamide gel electrophoresis. The Km values for CADCase/CSADCase are 0.22 and 0.18 mM with L-cysteic and cysteine sulfinic acids as substrates, respectively. CADCase/CSADCase cannot use L-glutamate as substrate. GADCase can use L-glutamate, L-cysteic, and cysteine sulfinic acid as substrates with Km values of 1.6, 5.4, and 5.2 mM, respectively. Antibodies against CADCase/CSADCase do not crossreact with GADCase preparations and vice versa. It is concluded that CADCase/CSADCase and GADCase are two distinct enzyme entities and they are responsible for the biosynthesis of taurine and gamma-aminobutyric acid, respectively.

Animals↗
PubMed2006

Homocysteine and other structurally-diverse amino thiols can alter pancreatic beta cell function without evoking cellular damage.

Homocysteine and related amino thiols, homocysteic acid, cysteic acid, homocysteine sulphinic acid and cysteine sulphinic acid have been labelled as neurotoxins. Homocysteine thiolactone, a metabolic derivative of homocysteine, is cytotoxic to endothelial cells and other cell lineages. Since pancreatic beta cells share many phenotypic similarities with neuronal cells, the present study uses clonal pancreatic BRIN-BD11 cells to investigate possible detrimental effects of these amino thiols on insulin secretion and pancreatic beta cell function. Insulin secretion was concentration-dependently inhibited at both basal (1.1 mM) and stimulatory (16.7 mM) glucose by homocysteine, homocysteine thiolactone and homocysteine sulphinic acid. Cysteic acid concentration-dependently inhibited insulin secretion at 16.7 mM glucose. Cell viability was not compromised by any of the amino thiols. Insulin secretory responses to alanine were inhibited by homocysteine, homocysteine thiolactone, homocysteic acid and cysteic acid. Insulin secretion in the presence of elevated Ca(2+) and forskolin were lowered by all amino thiols, except homocysteic acid. The secretory responsiveness to PMA, GLP-1 and KCl were only impaired in the presence of homocysteine and homocysteine thiolactone. These findings indicate that homocysteine, homocysteine thiolactone and, to a lesser extent, other amino thiols cause dysfunctional insulin secretion from pancreatic beta cells.

Animals↗