Zobrazeno 1 - 6
of 6
pro vyhledávání: '"D. W. Gottschall"'
Publikováno v:
ACS Symposium Series ISBN: 9780841224728
Xenobiotics and Food-Producing Animals: Metabolism and Residues
Xenobiotics and Food-Producing Animals: Metabolism and Residues
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f20e7148d0ad2705dc47e24cadc8e576
https://doi.org/10.1021/bk-1992-0503.ch010
https://doi.org/10.1021/bk-1992-0503.ch010
Autor:
R A, Lazarus, D E, Wallick, R F, Dietrich, D W, Gottschall, S J, Benkovic, B J, Gaffney, R, Shiman
Publikováno v:
Federation proceedings. 41(9)
The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an interme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a956607177ff3520adec1559889193d0
https://pubmed.ncbi.nlm.nih.gov/6282659
https://pubmed.ncbi.nlm.nih.gov/6282659
Publikováno v:
Chemischer Informationsdienst. 13
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0181e42afee7ba68310eb3f286d877b5
https://doi.org/10.1002/chin.198244088
https://doi.org/10.1002/chin.198244088
Publikováno v:
The Journal of biological chemistry. 257(2)
Phenylalanine hydroxylase requires 1.0 mol of iron/Mr = 50,000 subunit for maximal activity. A direct correlation between iron content and specific activity has been demonstrated through a comparison of enzyme activity and iron bound per subunit for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bc9a58594f3fe8380288ec6443226acd
https://pubmed.ncbi.nlm.nih.gov/7054185
https://pubmed.ncbi.nlm.nih.gov/7054185
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 16(6)
The antibiotic virginiamycin (VM) was extensively metabolized in cattle rumen fluid in vitro. The antimicrobial activity of VM decreased rapidly with an initial half-life of approximately 8 hr. In contrast, in buffer at near neutral pH, VM maintained
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bfbbae3ee0a87ef8e4ff6cbca19a7c60
https://pubmed.ncbi.nlm.nih.gov/2907457
https://pubmed.ncbi.nlm.nih.gov/2907457
Autor:
D. H. HUTSON, G. D. PAULSON, D. R. HAWKINS, C. B. STRUBLE, K. N. Woodward, N. E. Weber, R. P. Clement, R. D. Simmons, R. J. Christopher, S. F. Charles, C. N. Casciano, C. B. McCullough, J. F. Lamendola, M. N. Cayen, M. J. Lynch, G. M. Frame, J. F. Ericson, E. F. Illyes, M. A. Nowakowski, L. A. P. Hoogenboom, M. B. M. Huveneers-Oorsprong, H. A. Kuiper, J. E. Riviere, Kevin M. Kleinow, Margaret O. James, John J. Lech, R. E. Hornish, T. S. Arnold, L. Baczynskyj, S. T. Chester, T. D. Cox, T. F. Flook, R. L. Janose, D. A. Kloosterman, J. M. Nappier, D. R. Reeves, F. S. Yein, M. J. Zaya, M. Y. K. Ho, D. W. Gottschall, R. Wang, A. L. Donoho, T. D. Thomson, D. D. Giera, Jinn Wu, Dave D. W. Liu, Robert A. Robinson, William Itterly, Thomas M. Capps, V. J. Feil, P. J. Sommer, C. H. Lamoureux, Bruce A. Halley, Narayana I. Narasimhan, Kalpana Venkataraman, Rae Taub, Marilyn L. G. Erwin, Nicholas W. Andrew, Peter G. Wislocki, C. A. Weerasinghe, E. Warrakah, S. Shuman, J. E. Dalidowicz, G. E. Babbitt