Zobrazeno 1 - 7
of 7
pro vyhledávání: '"K M, Kedzie"'
Publikováno v:
Journal of Biological Chemistry. 265:3648-3653
We have cloned the gene for human interstitial retinol-binding protein (IRBP) and compared its nucleotide sequence with that of the corresponding cloned cDNA. The human IRBP gene is approximately 9.5 kilobase pairs (kbp) in length and consists of fou
Autor:
J W, Regan, T J, Bailey, D J, Pepperl, K L, Pierce, A M, Bogardus, J E, Donello, C E, Fairbairn, K M, Kedzie, D F, Woodward, D W, Gil
Publikováno v:
Molecular pharmacology. 46(2)
A cDNA that when expressed has the binding and functional characteristics of the pharmacologically defined EP2 prostaglandin (PG) receptor [Cardiovasc. Drug Rev. 11:165-179 (1993)] has been cloned from a human placenta library. This clone, known as H
Autor:
J A, Hasler, G R, Harlow, G D, Szklarz, G H, John, K M, Kedzie, V L, Burnett, Y A, He, L S, Kaminsky, J R, Halpert
Publikováno v:
Molecular pharmacology. 46(2)
Eleven amino acid residues unique to dog cytochrome P450 (P450) 2B11, compared with rat 2B1 and 2B2, rabbit 2B4 and 2B5, and mouse 2B10, in the putative substrate recognition sites [J. Biol. Chem. 267:83-90 (1992)] were mutated to the residues found
Autor:
K M, Kedzie, C A, Balfour, G Y, Escobar, S W, Grimm, Y A, He, D J, Pepperl, J W, Regan, J C, Stevens, J R, Halpert
Publikováno v:
The Journal of biological chemistry. 266(33)
Liver microsomes from phenobarbital-treated rats of four inbred strains expressing distinct allelic variants of cytochrome P450IIB1 were analyzed. The Wistar Munich (WM) strain exhibited 5- to 10-fold lower androstenedione 16 beta-hydroxylase activit
Publikováno v:
The Journal of biological chemistry. 265(7)
We have cloned the gene for human interstitial retinol-binding protein (IRBP) and compared its nucleotide sequence with that of the corresponding cloned cDNA. The human IRBP gene is approximately 9.5 kilobase pairs (kbp) in length and consists of fou
Publikováno v:
Journal of Biological Chemistry. 264:16629-16637
The aspartate transcarbamoylases (ATCase, EC 2.1.3.2) of Escherichia coli and Serratia marcescens have similar dodecameric enzyme structures (2(c3):3(r2] but differ in both regulatory and catalytic characteristics. The catalytic cistrons (pyrB) of th
Publikováno v:
The Journal of biological chemistry. 264(28)
The aspartate transcarbamoylases (ATCase, EC 2.1.3.2) of Escherichia coli and Serratia marcescens have similar dodecameric enzyme structures (2(c3):3(r2] but differ in both regulatory and catalytic characteristics. The catalytic cistrons (pyrB) of th