Molecular characterization of monoamine oxidases A and B

Autor: C W, Abell, S W, Kwan

Publikováno v: Progress in nucleic acid research and molecular biology. 65

Monoamine oxidase A and B (MAO A and B) are the major neurotransmitter-degrading enzymes in the central nervous system and in peripheral tissues. MAO A and B cDNAs from human, rat, and bovine species have been cloned and their deduced amino acid sequ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::235ef191af1cc19e2e00aad703b08387
https://pubmed.ncbi.nlm.nih.gov/11008487

Molecular properties of monoamine oxidases A and B

Autor: J. M. Bergeron, Sau-Wah Kwan, C. W. Abell

Publikováno v: Psychopharmacology.

Monoamine oxidases A and B (MAO-A and B) catalyze the oxidative catabolism of biogenic amines and xenobiotics. Investigation of these mitochondrial membrane proteins shows that they differ in substrate preference, inhibitor specificity, tissue and ne

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b253c95dc50143fc065999b4c8d5329
https://pubmed.ncbi.nlm.nih.gov/1546120

Monoclonal antibodies and immobilized antibodies

Autor: Robert J. Linhardt, C. W. Abell, R. M. Denney, B. W. Altrock, R. Auerbach, S. D. Bernal, R. E. Canfield, P. H. Ehrlich, W. R. Moyle, T. S. Chan, T. W. Chang, N. T. Chang, J. A. Cidlowski, M. D. Viceps, R. J. Cote, D. M. Morrissey, A. N. Houghton, E. J. Beattie, H. F. Oettgen, L. J. Old, C. M. Croce, R. S. Cubicciotti, A. E. Karu, R. M. Krauss, J. S. Cullor, A. Deutsch, H. Brandwein, H. Platt, D. M. Hunter, A. Dubitsky, S. M. Durham, F. A. Dolbeare, J. W. Gray, G. R. Dreesman, C. E. Kendall, J. C. Egrie, A. R. Frackelton, H. N. Eisen, A. H. Ross, S. Gay, G. Geirnaert, J. E. Geltosky, E. H. Goldberg, E. Goldwasser, C. Kavinsky, T. L. Weiss, H. G. Gratzner, B. Hampar, M. Zweig, S. D. Showalter, H. H. Handley, M. C. Glassy, Y. Hagiwara, H. Hagiwara, C. M. Huang, S. N. Cohen, J. V. Hughes, E. M. Scolnick, J. E. Tomassini, R. Jefferis, J. Steensgaard, H. S. Kaplan, N. N. H. Teng, K. S. Earn, R. F. Calvo, L. Kass, J. R. Kettman, M. V. Norgard, M. B. Khazaeli, W. H. Beierwaltes, B. G. England, P. C. Kung, G. Goldstein, L. Lanier, J. Phillips, N. L. Warner, J. W. Larrick, A. R. Raubitschek, K. E. Truitt, H. Lazarus, J. F. Schwaber, J. Lewicki, C. Lewis, J. V. Olander, W. R. Tolbert, E. L. Milford, C. B. Carpenter, J. M. Paradysz, D. F. Mosher, J. L. Mulshine, J. D. Minna, K. A. Murray, D. M. Neville, R. J. Youle, M. Nicolson, I. Pastan, M. C. Willingham, D. J. Fitzgerald, A. Pucci, A. M. Smithyman, M. B. Slade, P. W. French, G. Wijffels, C. S. Pukel, K. O. Lloyd, L. R. Travassos, W. G. Dippold, R. P. Reckel, J. L. Harris, R. Wellerson, S. M. Shaw, P. M. Kaplan, E. L. Reinherz, S. F. Schlossman, S. C. Mener, J. Sakamoto, C. C. Cordon, E. Friedman, C. L. Finstad, W. E. Enker, M. R. Melamed, J. F. Oettgen, P. J. Scannon, L. E. Spitler, H. M. Lee, R. T. Kawahata, R. P. Mischak, J. Schlom, D. Colcher, M. Nuti, P. H. Hand, F. Austin, G. D. Shockman, D. E. Jackson, W. Wong, Z. Steplewski, H. Koprowski, M. Herlyn, M. Strand, I. S. Trowbridge, D. L. Urdal, C. J. March, S. K. Dower, J. R. Wands, V. R. Zurawski, C. A. White, R. Dulbecco, W. R. Allen, E. C. Arnold, M. Flasher, H. H. Freedman, T. D. Heath, P. Shek, D. Papahadjopoulos, M. Ikeda, S. Sakamoto, K. Suzuki, M. Kuboyama, Y. Harada, A. Kawashiri, E. Takahashi, H. S. Lee, S. Margel, R. C. Nowinski, A. S. Hoffman, J. W. Peterson, K. B. Platt, D. E. Reed, F. X. Real, M. J. Mattes, P. O. Livingston, A. Rembaum, R. C. K. Yen, R. Rosenstein, B. Schneider

Publikováno v: Applied Biochemistry and Biotechnology. 15:53-80

Antibodies in both their free and immobilized state have been the object of considerable industrial and academic interest. A variety of methods are used for preparing and immobilizing antibodies. Applications for monoclonal antibodies include the pre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::53b3e2a60fa089ffc4619eece666554b
https://doi.org/10.1007/bf02798506

Phenylalanine ammonia-lyase. Induction and purification from yeast and clearance in mammals

Autor: C W Abell, R R Fritz, D S Hodgins

Publikováno v: Journal of Biological Chemistry. 251:4646-4650

Yeast phenylalanine ammonia-lyase (EC 4.3.1.5) catalyzes the deamination of L-phenylalanine to form trans-cinnamic acid and tyrosine to trans-coumaric acid. Maximal enzyme activity in Rhodotorula glutinis (2 units/g, wet weight, of yeast) was induced

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a083bb39430af6900aeb6da8d2dfe803
https://doi.org/10.1016/s0021-9258(17)33251-9

The Stability of Polyuridylic Acid in Acid Solution*

Autor: D. H. Rammler, C. W. Abell, A. Delk

Publikováno v: Biochemistry. 4:2002-2009

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c1a8d531101c32d7ccb658711616a486
https://doi.org/10.1021/bi00886a014