Detail of "1113-41-3"

Reference

Molecular biological studies with 14C-D-penicillamine and 14C-L-penicillamine

Molecular biological studies with 14C-D-penicillamine and 14C-L-penicillamine. Lodemann, E.; Ulrich, P.; Wacker, Adolf (Inst. Ther. Biochem., Frankfurt/Main, Ger.). D-Penicillamin, 163-6, 189-216. Edited by: Kreysel, Hans-Wilhelm. Schattauer: Stuttgart, Ger. (German) 1977. CODEN: 37GDAT. DOCUMENT TYPE: Conference CA Section: 1 (Pharmacodynamics) 14C-labeled L-penicillamine [1113-41-3] was incorporated into mouse L cells and human embryonic fibroblasts to a greater extent than was D-penicillamine [52-67-5]. The binding of L-penicillamine-14C by tRNA from rat liver was decreased by 50% by addn. to the medium of L-penicillamine or valine, by 25% by isoleucine, and by 7% by leucine.

Disulfide reduction and sulfhydryl uptake by Streptococcus mutans

Disulfide reduction and sulfhydryl uptake by Streptococcus mutans. Thomas, Edwin L. (Dep. Biochem., St. Jude Child. Res. Hosp., Memphis, TN 38101, USA). J. Bacteriol., 157(1), 240-6 (English) 1984. CODEN: JOBAAY. ISSN: 0021-9193. DOCUMENT TYPE: Journal CA Section: 10 (Microbial Biochemistry) Incubation of S. mutans cells with certain disulfide compds. resulted in accumulation of reduced sulfhydryl compds.Several reagents with their cas registry numbers 56-41-7 and 1113-41-3 are used here. in the extracellular medium or in both the medium and the cells. Oxidized lipoic acid and lipoamide competed for redn. At high concns., these compds. were reduced at rates comparable to that of glucose metab., and all of the increase in sulfhydryls was in the medium. Cystamine did not compete with these compds. for redn. but was also reduced at high rates and low apparent affinity, and all of the cysteamine produced from cystamine accumulated in the medium. In contrast, glutathione disulfide (GSSG) and L-cystine were reduced slowly but with high apparent affinity, and 60-80% of the increase in sulfhydryls was intracellular. NADH-dependent lipoic acid or lipoamide reductase activity was present in the particulate (wall-plus-membrane) fraction, whereas NADPH-dependent GSSG reductase activity was present in the sol. (cytoplasmic) fraction. Two transport systems for disulfide and sulfhydryl compds. were distinguished. GSSG, L-cystine, and reduced glutathione competed for uptake. L-Cysteine was taken up by a sep. system that also accepted L-penicillamine and D-cysteine as substrates. Uptake of glutathione or L-cysteine, or the uptake and redn. of GSSG or L-cystine, resulted in up to a 10-fold increase in cell sulfhydryl content that raised intracellular concns. to 30-40 mM. These reductase and transport systems enable S. mutans cells to create a reducing environment in both the extracellular medium and the cytoplasm. .