نتایج جستجو برای: microsomal enzyme depen dent polymers

تعداد نتایج: 319118  

Journal: :The Journal of biological chemistry 1969
S Mahadevan F Sauer

Rat liver, kidney, pancreas, and small intestine have enzymes which hydrolyze fatty acid esters of carnitine. The liver enzyme, located in the microsomal fraction, was solubilized by sonic disruption and purified l&fold by diethylaminoethyl cellulose chromatography and Sephadex gel filtration. The purified enzyme sedimented in the ultracentrifuge as a single protein with an szo+, of 4.5 S. The ...

Journal: :Langmuir 2021

Lubricant-infused surfaces (LIS) have emerged as an innovative way to combat several modern challenges such biofouling, ice formation, and surface drag. The favorable properties of LIS are depen...

Journal: :The Biochemical journal 1979
C A Lamartiniere C S Dieringer E Kita G W Lucier

The hepatic microsomal enzyme UDP-glucuronyltransferase undergoes a complex developmental pattern in which enzyme activity is first detectable on the 18th day of gestation in rats. Prepubertal activities are similar for males and females. However, postpubertal sexual differentiation of enzyme activity occurs in which male activities are twice those of females. Neonatal administration of testost...

Journal: :Journal of lipid research 1981
S K Erickson B Bösterling

Cholesterol 7 alpha-hydroxylase, the rate-limiting enzyme for bile acid synthesis, was shown to be copurified with human liver microsomal cytochrome P-450. When these cytochrome P-450 species were reconstituted in phospholipid-cholesterol vesicles together with NADPH-cytochrome P-450 reductase, high cholesterol 7 alpha-hydroxylase activity was obtained in the presence of NADPH. The activity rep...

Journal: :The Journal of biological chemistry 1962
A H PHILLIPS R G LANGDON

has previously been isolated by Horecker (1) from an acetone powder of liver and characterized as a flavoprotein. It was initially suggested that this enzyme was localized in hepatic mitochondria. However, subsequent studies have revealed that triphosphopyridine nucleotide-cytochrome c reductase activity is also present in hepatic microsomes (a), and it has been reported that the properties of ...

Journal: :The Journal of biological chemistry 1968
S V Pande J F Mead

The inhibition of several enzyme activities by free fatty acids has been examined. The inhibition of rat liver microsomal linolenate-activating enzyme activity by linolenate was found to be due to the inactivation of enzyme by substrate fatty acid. Stearoyl coenzyme A was also found to inhibit linolenate-activating enzyme. Likewise, microsomal glucose 6-phosphatase was inhibited by oleate; the ...

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