The Kinetic Properties of Oleoyl-CoA:1-Acyl-sn-glycero-3-phosphocholine O-Acyltransferase from Mouse-Brain Microsomes

Histamine N-methyltransferase (EC 2.1.1.8) was purified 1100-fold from ox brain. The native enzyme has an Mr of 34800 +/- 2400 as measured by gel filtration on Sephadex G-100. The enzyme is highly specific for histamine. It does not methylate noradrenaline, adrenaline, DL-3,4-dihydroxymandelic acid, 3,4-dihydroxyphenylacetic acid, 3-hydroxytyramine or imidazole-4-acetic acid. Unlike the enzyme from rat and mouse brain, ox brain histamine N-methyltransferase did not exhibit substrate inhibition by histamine. Initial rate and product inhibition studies were consistent with an ordered steady-state mechanism with S-adenosylmethionine being the first substrate to bind to the enzyme and N-methylhistamine being the first product to dissociate.

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Nervonic acid biosynthesis by erucyl-coa elongation in normal and quaking mouse brain microsomes. Elongation of other unsaturated fatty acyl-CoAs (mono and polyunsaturated)

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism ◽

10.1016/0005-2760(76)90043-6 ◽

1976 ◽

Vol 424 (1) ◽

pp. 1-7 ◽

Cited By ~ 53

Author(s):

Jean-Marie Bourre ◽

Odile Daudu ◽

Nicole Baumann

Keyword(s):

Mouse Brain ◽

Fatty Acyl ◽

Nervonic Acid ◽

Acid Biosynthesis ◽

Brain Microsomes

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CERAMIDE-GALACTOSYLTRANSFERASE AND CEREBROSIDE-SULPHOTRANSFERASE LOCALISATION IN GOLGI MEMBRANES ISOLATED BY A CONTINUOUS SUCROSE GRADIENT OF MOUSE BRAIN MICROSOMES

Journal of Neurochemistry ◽

10.1111/j.1471-4159.1979.tb05180.x ◽

1979 ◽

Vol 33 (2) ◽

pp. 497-504 ◽

Cited By ~ 47

Author(s):

H. P. Siegrist ◽

T. Burkart ◽

U. N. Wiesmann ◽

N. N. Herschkowitz ◽

M. A. Spycher

Keyword(s):

Mouse Brain ◽

Sucrose Gradient ◽

Golgi Membranes ◽

Continuous Sucrose Gradient ◽

Brain Microsomes

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High activity of cytochrome P-450-linked aminopyrine N-demethylase in mouse brain microsomes, and associated sex-related difference

Biochemical Journal ◽

10.1042/bj2610769 ◽

1989 ◽

Vol 261 (3) ◽

pp. 769-773 ◽

Cited By ~ 23

Author(s):

V Ravindranath ◽

H K Ananda Theertha Varada

Keyword(s):

Mouse Brain ◽

Male Mouse ◽

Mouse Liver ◽

Double Diffusion ◽

Microsomal Protein ◽

Cross Reactivity ◽

Related Difference ◽

Brain Microsomes ◽

Demethylase Activity ◽

Cytochrome P 450

The presence of cytochrome P-450 and associated mono-oxygenase activities was examined in brain microsomes from male and female mice. Although the cytochrome P-450 level in male mouse brain was very low as compared with mouse liver, the aminopyrine N-demethylase and morphine N-demethylase specific activities in male mouse brain were much higher than those observed in mouse liver. Ethoxycoumarin O-de-ethylase and aniline hydroxylase activities were, however, not detected in mouse brain. Sex-related differences were observed in both the cytochrome P-450 levels and aminopyrine N-demethylase activity in mouse brain, the levels of both being higher in male mouse brain as compared with female mouse brain. Aminopyrine N-demethylase activity in mouse brain microsomes was dependent on the presence of oxygen and NADPH and could be inhibited by piperonyl butoxide, N-octyl imidazole and carbon monoxide. Antiserum raised to the phenobarbital-inducible form of rat liver cytochrome P-450 [P-450(b+e)] inhibited mouse brain aminopyrine N-demethylase activity by around 80+ mouse brain microsomal protein exhibited cross-reactivity against this antiserum when examined by Ouchterlony double diffusion and immunoblotting. The present results indicate the presence of a phenobarbital-inducible form of cytochrome P-450 (or a form of cytochrome P-450 that is similar immunologically) in mouse brain microsomes, which is associated with a sex-related difference.

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