Gut J - Search Results

1

Debrisoquine/sparteine-type polymorphism of drug oxidation. Purification and characterization of two functionally different human liver cytochrome P-450 isozymes involved in impaired hydroxylation of the prototype substrate bufuralol.

Gut J, Catin T, Dayer P, Kronbach T, Zanger U, Meyer UA. Gut J, et al. J Biol Chem. 1986 Sep 5;261(25):11734-43. J Biol Chem. 1986. PMID: 3745165 Free article.

2

The molecular mechanisms of two common polymorphisms of drug oxidation--evidence for functional changes in cytochrome P-450 isozymes catalysing bufuralol and mephenytoin oxidation.

Meyer UA, Gut J, Kronbach T, Skoda C, Meier UT, Catin T, Dayer P. Meyer UA, et al. Among authors: gut j. Xenobiotica. 1986 May;16(5):449-64. doi: 10.3109/00498258609050251. Xenobiotica. 1986. PMID: 2874666

3

Debrisoquine-type polymorphism of drug oxidation: purification from human liver of a cytochrome P450 isozyme with high activity for bufuralol hydroxylation.

Gut J, Gasser R, Dayer P, Kronbach T, Catin T, Meyer UA. Gut J, et al. FEBS Lett. 1984 Aug 6;173(2):287-90. doi: 10.1016/0014-5793(84)80792-9. FEBS Lett. 1984. PMID: 6146537 Free article.

4

Mephenytoin-type polymorphism of drug oxidation: purification and characterization of a human liver cytochrome P-450 isozyme catalyzing microsomal mephenytoin hydroxylation.

Gut J, Meier UT, Catin T, Meyer UA. Gut J, et al. Biochim Biophys Acta. 1986 Dec 10;884(3):435-47. doi: 10.1016/0304-4165(86)90194-7. Biochim Biophys Acta. 1986. PMID: 3096378

5

High-performance liquid chromatographic assays for bufuralol 1'-hydroxylase, debrisoquine 4-hydroxylase, and dextromethorphan O-demethylase in microsomes and purified cytochrome P-450 isozymes of human liver.

Kronbach T, Mathys D, Gut J, Catin T, Meyer UA. Kronbach T, et al. Among authors: gut j. Anal Biochem. 1987 Apr;162(1):24-32. doi: 10.1016/0003-2697(87)90006-6. Anal Biochem. 1987. PMID: 3605590

6

Characterization of a common genetic defect of cytochrome P-450 function (debrisoquine-sparteine type polymorphism)--increased Michaelis is Constant (Km) and loss of stereoselectivity of bufuralol 1'-hydroxylation in poor metabolizers.

Dayer P, Gasser R, Gut J, Kronbach T, Robertz GM, Eichelbaum M, Meyer UA. Dayer P, et al. Among authors: gut j. Biochem Biophys Res Commun. 1984 Nov 30;125(1):374-80. doi: 10.1016/s0006-291x(84)80378-2. Biochem Biophys Res Commun. 1984. PMID: 6508804

7

Genomics and the prediction of xenobiotic toxicity.

Meyer UA, Gut J. Meyer UA, et al. Among authors: gut j. Toxicology. 2002 Dec 27;181-182:463-6. doi: 10.1016/s0300-483x(02)00452-3. Toxicology. 2002. PMID: 12505353 Review.

8

Rotation of cytochrome P-450. I. Investigations of protein-protein interactions of cytochrome P-450 in phospholipid vesicles and liver microsomes.

Kawato S, Gut J, Cherry RJ, Winterhalter KH, Richter C. Kawato S, et al. Among authors: gut j. J Biol Chem. 1982 Jun 25;257(12):7023-9. J Biol Chem. 1982. PMID: 7085615 Free article.

9

Rotation of cytochrome P-450. Complex formation of cytochrome P-450 with NADPH-cytochrome P-450 reductase in liposomes demonstrated by combining protein rotation with antibody-induced cross-linking.

Gut J, Richter C, Cherry RJ, Winterhalter KH, Kawato S. Gut J, et al. J Biol Chem. 1983 Jul 25;258(14):8588-94. J Biol Chem. 1983. PMID: 6408090 Free article.

These results further support the proposal of the formation of monomolecular complexes between cytochrome P-450 and NADPH-cytochrome P-450 reductase in liposomal membranes (Gut, J., Richter, C., Cherry, R.J., Winterhalter, K.H., and Kawato, S. (1982) J …

These results further support the proposal of the formation of monomolecular complexes between cytochrome P-450 and NADPH-cytochrome P-450 r …

10

Rotation of cytochrome P-450. II. Specific interactions of cytochrome P-450 with NADPH-cytochrome P-450 reductase in phospholipid vesicles.

Gut J, Richter C, Cherry RJ, Winterhalter KH, Kawato S. Gut J, et al. J Biol Chem. 1982 Jun 25;257(12):7030-6. J Biol Chem. 1982. PMID: 6806262 Free article.

The rotational mobility of cytochrome P-450, when reconstituted alone, was found to be dependent on the lipid to protein ratio by weight (L/P450) (Kawato, S., Gut, J., Cherry, R. J., Winterhalter, K. H., and Richter, C. (1982) J. Biol. Chem. 257, 7023- …

The rotational mobility of cytochrome P-450, when reconstituted alone, was found to be dependent on the lipid to protein ratio by weight (L/ …

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