نتایج جستجو برای: microsomal enzyme depen dent polymers

تعداد نتایج: 319118  

Journal: :The Biochemical journal 1981
O Nygård T Hultin

1. After dimethylnitrosamine (DMNA) administration to mice, the content of poly(A)-containing RNA decreases rapidly in the postmicrosomal fraction of the liver. We report here that the loss of free mRNA is not a result of increased nucleolytic activity. On the contrary, a decreased activity of microsomal endonuclease, assayed by its effect on polyribosomal mRNA, was demonstrated already 15 min ...

Journal: :Japanese journal of pharmacology 1985
S Sugiyama M Hosokawa T Igarashi K Ueno T Satoh H Kitagawa

Inhibition of rat liver microsomal carboxylesterase (CEase) by O-ethyl O-p-nitrophenyl phenylphosphonothioate (EPN) and binding of EPN oxygen analog to microsomal CEase were enhanced by addition of NAD or NADP. This was more prominent in addition of NAD than NADP. No potentiation of anti-CEase action of EPN by NAD was seen when pure esterase (E.C. 3.1.1.1) instead of liver microsomes was used a...

Journal: :Biological & pharmaceutical bulletin 2001
S Narimatsu T Arai Y Masubuchi T Horie M Hosokawa K Ueno H Kataoka S Yamamoto T Ishikawa A K Cho

Repetitive administration of propranolol (PL) in rats decreases the activities of cytochrome P450 (CYP) 2D enzyme(s) in hepatic microsomes. We examined the properties of 4-hydroxypropranolol (4-OH-PL) as an inactivator of rat liver microsomal CYP2D enzyme(s) using bunitrolol (BTL) 4-hydroxylation and PL 5- and 7-hydroxylations as indices of CYP2D enzyme activity. Rat microsomal BTL 4-hydroxylas...

Journal: :The Journal of biological chemistry 1991
C Andersson E Mosialou A E Adang G J Mulder A van der Gen R Morgenstern

The substrate specificity of rat liver microsomal glutathione transferase toward glutathione has been examined in a systematic manner. Out of a glycyl-modified and eight gamma-glutamyl-modified glutathione analogues, it was found that four (glutaryl-L-Cys-Gly, alpha-L-Glu-L-Cys-Gly, alpha-D-Glu-L-Cys-Gly, and gamma-L-Glu-L-Cys-beta-Ala) function as substrates. The kinetic parameters for three o...

Journal: :The Biochemical journal 1995
N M Broadway E D Saggerson

Conditions have been developed for the solubilization of hepatic microsomal carnitine acyltransferase activity in good yield, with excellent long-term stability and with retention of malonyl-CoA sensitivity. Solubilized microsomal carnitine acyltransferase activity can be separated into malonyl-CoA-sensitive and -insensitive activities either by gel filtration on Superdex 200 or by anion-exchan...

Journal: :Japanese journal of pharmacology 1994
Y Aniya A Daido

The activation of microsomal glutathione S-transferase in oxidative stress was investigated by perfusing isolated rat liver with 1 mM tert-butyl hydroperoxide (t-BuOOH). When the isolated liver was perfused with t-BuOOH for 7 min and 10 min, microsomal, but not cytosolic, glutathione S-transferase activity was increased 1.3-fold and 1.7-fold, respectively, with a concomitant decrease in glutath...

Journal: :The Journal of Cell Biology 1977
O S Nilsson G Dallner

The transverse distribution of enzyme proteins and phospholipids within microsomal membranes was studied by analyzing membrane composition after treatment with proteases and phospholipases. Upon trypsin treatment of closed microsomal vesicles, NADH- and NADPH-cytochrome c reductases as well as cytochrome b5 were solubilized or inactivated, while cytochrome P-450 was partially inactivated. When ...

Journal: :The Journal of Biophysical and Biochemical Cytology 1957
K. Bruce Jacobson Nathan O. Kaplan

1. The distribution of DPN and DPNH pyrophosphatases and DPNase in centrifugally prepared fractions of organs of several species of animals is reported. 2. A DPNH pyrophosphatase was found in the soluble fraction of pigeon and of rabbit liver. This enzyme did not split DPN but accounted for over 50 per cent of the DPNH pyrophosphatase activity of the whole homogenates. 3. All the organs tested,...

Journal: :The Journal of biological chemistry 1984
T C Linn P A Srere

Purified rat liver ATP citrate lyase is shown to bind to the microsomal fraction of rat liver. Under the same conditions the enzyme does not bind significantly to the mitochondrial fraction or to the outer membrane prepared from the mitochondrial fraction. The binding component of the microsomal fraction is further identified as the endoplasmic reticulum, and a protein component of the membrane...

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