Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Nakanishi A"'
Publikováno v:
Journal of biochemistry. 147(2)
Endogenous phosphatidylcholine in biological membranes exists as isomers with acyl moieties at the sn-1 or sn-2 positions of the glycerol backbone. However, detailed biochemical information on these positional isomers is not generally available. This
Publikováno v:
Journal of biochemistry. 145(1)
The liver is a unique organ with the potential to regenerate from injury. Hepatic stem cells contribute to liver regeneration when surviving hepatocytes in injured liver are unable to proliferate. To investigate the mechanism of liver regeneration in
Publikováno v:
Journal of biochemistry. 115(2)
An extramitochondrial acetyl-CoA hydrolase [EC 3.1.2.1] in the rat liver, which is stimulated by ATP and inhibited by ADP, is known to be extremely cold-labile. During subcellular fractionations at low temperatures (2-4 degrees C), most of the enzyme
Autor:
Hirata, Mitsuhi, Amano, Kumiko, Miyashita, Ayumi, Yasunaga, Mayu, Nakanishi, Tomoko, Sato, Kenzo
Publikováno v:
Journal of Biochemistry; Jan2009, Vol. 145 Issue 1, p51-58, 8p, 1 Chart, 4 Graphs
Publikováno v:
Journal of biochemistry. 81(3)
An enzyme designated as NADPH-dihydropteridine reductase was found in the extract of bovine liver and partially purified. In contrast to NADH-dpendent dihydropteridine reductase [EC 1.6.99.7], the enzyme catalyzes the reduction of quinonid-dihydropte
Publikováno v:
Journal of biochemistry. 99(5)
It has been difficult to determine exactly NADPH-specific dihydropteridine reductase [EC 1.6.99.10] in samples which also contain NADH-specific dihydropteridine reductase [EC 1.6.99.7], because the latter enzyme interferes with the activity measureme
Publikováno v:
Journal of biochemistry. 88(3)
When rat liver cytoplasm free of glucocorticoid receptors was dialyzed, its inhibitory effect on nuclear uptake or binding of already "activated" receptor-glucocorticoid complex increased. A macromolecular fraction and a low-molecular-weight fraction
Publikováno v:
Journal of biochemistry. 106(5)
The mechanism of inhibition of aminopeptidase M by bile acids was analyzed by application of the specific velocity plot that was introduced by Baici [Eur. J. Biochem. 119, 9-14 (1981)]. Kinetic studies with three bile acids (cholic acid, deoxycholic