Results 221 to 230 of about 64,891 (274)
Some of the next articles are maybe not open access.
Chromate metabolism in liver microsomes
Biological Trace Element Research, 1979The carcinogenicity and mutagenicity of various chromium compounds have been found to be markedly dependent on the oxidation state of the metal. The carcinogen chromate was reduced to chromium(III) by rat liver microsomes in vitro. Metabolism of chromate by microsomal enzymes occurred only in the presence of either NADPH or NADH as cofactor.
openaire +2 more sources
Pigments of rat liver microsomes
Archives of Biochemistry and Biophysics, 1958Abstract The total hemin content of washed rat liver microsomes is 2.15 times the cytochrome b5 content, only a small part being due to bound hemoglobin. The content of flavine is 4 5 that of cytochrome b5. The flavine probably does not contribute to the DPNH reduced difference spectrum.
openaire +3 more sources
Kavalactone Metabolism in Rat Liver Microsomes
Phytotherapy Research, 2011The specific CYP enzymes involved in kavalactone (KLT) metabolism and their kinetics have not been fully examined. This study used rat liver microsomes (RLM) to determine kavain (KA), methysticin (MTS) and desmethoxyyangonin (DMY) enzyme kinetic parameters, to elucidate the major CYP450 isoforms involved in KLT metabolism and to examine gender ...
Shuang, Fu, Anthony, Rowe, Iqbal, Ramzan
openaire +2 more sources
FRACTIONATION OF MOUSE LIVER MICROSOMAL ESTERASES
Canadian Journal of Biochemistry, 1965Mouse liver microsomal esterases were fractionated on DEAE-cellulose after the solution of these enzymes in a solution containing 0.1 M glycyl glycine buffer, pH 7.0, and 5 × 10−4 M Lubrol W, a nonionic detergent. Elution of the enzymes from the DEAE-cellulose was accomplished by using NaCl in the glycyl glycine – Lubrol W solution.
C, CARRUTHERS, E, HEINS, A, BAUMLER
openaire +2 more sources
A microsomal exoribonuclease from rat liver
Biochimica et Biophysica Acta (BBA) - Enzymology, 1979A exoribonuclease has been purified from the microsomes of rat liver. The enzyme had an apparent molecular weight of 80 000-83 000 and produced, via a processive mechanism, 5'-AMP as the only product from poly(A). The degradation was found to proceed in the 3' to 5' direction.
H, Kumagai +4 more
openaire +2 more sources
Lipid peroxidation of rat liver microsomes
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 19801. The NADPH-dependent lipid peroxidation process was studied with microsomes and also the effects of addition of superoxide dismutase, catalase and thiourea. Only catalase and thiourea were able to inhibit lipid peroxidation. It seems that the initiating radical is the OH. radical formed by the Fenton reaction. 2.
J F, Koster, R G, Slee
openaire +2 more sources
Mannosyltransfer reactions in rabbit liver microsomes
Biochemical and Biophysical Research Communications, 1976Abstract Rabbit liver microsomes catalyzed mannosyltransfer from GDP-[14C]mannose to free D -mannose resulting in the synthesis of α-1,2-, α-1,3-, and α-1,6-mannosyl-mannose. Whereas formation of α-1,2-mannosyl-mannose was stimulated by the addition of manganese chloride or nickel chloride and was inhibited by EDTA, synthesis of α-1,3-mannosyl ...
J S, Schutzbach, A K, Verma
openaire +2 more sources
Phosphatidylcholine mobility in liver microsomal membranes
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1978Purified phosphatidylcholine exchange protein from bovine liver was used to exchange rat liver microsomal phosphatidylcholine for egg phosphatidylcholine. It was found that at 25 and 37 degrees C rat liver microsomal phosphatidylcholine was completely and rapidly available for replacement by egg phosphatidylcholine.
A M, van den Besselaar +3 more
openaire +2 more sources
Reversible inactivation of liver microsomal pyrophosphatese
Life Sciences, 1972Abstract Rat liver microsomes lost their pyrophosphatase activity in a pH and temperature dependent reaction. Peroxidation of microsomal lipids did not appear to be required as inactivation occured in the absence of measurable lipid peroxidation. The pH of the media affected the final extent of enzyme inactivation.
G W, Rafter, B H, Witherspoon
openaire +2 more sources
Gliclazide hydroxylation by rat liver microsomes
Xenobiotica, 19951. The metabolism of gliclazide to hydroxygliclazide has been investigated in Sprague-Dawley rat liver microsomes. 2. The kinetics of hydroxygliclazide formation are consistent with Michaelis-Menten kinetics (mean (+/- SD, n = 3) apparent K(m) and Vmax = 256 +/- 27 microM and 1.85 +/- 0.10 nmol/ min/mg respectively). 3.
A, Rieutord +3 more
openaire +2 more sources