Zobrazeno 1 - 10
of 64
pro vyhledávání: '"A F, Riggs"'
Publikováno v:
International Journal of Pharmaceutical and Healthcare Marketing. 10:161-191
Purpose The purpose of this research is to develop a taxonomy of the impact of sales process regulations, guidance statements and laws (henceforth, referred to as “regulations”) on sales behaviours within the pharmaceutical industry, particularly
Publikováno v:
The FASEB Journal. 27
Publikováno v:
Journal of the American Water Resources Association. 29:891-900
This study integrates an Agricultural Non-Point Source Pollution Model (AGNPS), the Geographic Resource Analysis Support System (GRASS) (U.S. Army Corps of Engineers, 1987), and GRASS WATERWORKS (a hydrologic modeling tool box being developed at the
Autor:
Lei-Ting Tam, D. J. Smith, A. F. Riggs, T. O. Baldwin, P. R. Kolatkar, R. H. Broyles, Bruce A. Roe, Hao Zhu
Publikováno v:
Journal of Biological Chemistry. 268:26961-26971
The adult bullfrog (Rana catesbeiana) has two major tetrameric hemoglobins, B and C, which share a common beta chain but have different alpha chains. Components B and C associate upon deoxygenation to form a complex of the form BC2, a trimer of tetra
Autor:
Mitra S, Rana, Austen F, Riggs
Publikováno v:
Proteins. 79(5)
The minor tetrameric hemoglobin (Hb), Hb D, of chicken red blood cells self-associates upon deoxygenation. This self-association enhances the cooperativity of oxygen binding. The maximal Hill coefficient is greater than 4 at high Hb concentrations. P
Autor:
Austen F. Riggs
Publikováno v:
American Zoologist. 31:535-545
Hemoglobins, found in members of almost all invertebrate phyla, display an extraordinary diversity of form and function. Although some are intracellular with chains and assemblies similar in size to those of vertebrates, others are giant extracellula
Autor:
Thomas L, Vandergon, Austen F, Riggs
Publikováno v:
Methods in enzymology. 436
Hemoglobins (Hbs) found in members of the phylum Nemertea are smaller than any other known Hb molecules. These mini-Hbs have been of great interest because of their unique three-dimensional structure and their stable ligand-binding properties. Also o
Publikováno v:
The Journal of biological chemistry. 275(41)
Widely distributed flavohemoglobins (flavoHbs) function as NO dioxygenases and confer upon cells a resistance to NO toxicity. FlavoHbs from Saccharomyces cerevisiae, Alcaligenes eutrophus, and Escherichia coli share similar spectra, O(2), NO, and CO
Publikováno v:
The Journal of biological chemistry. 275(18)
Lampreys, among the most primitive living vertebrates, have hemoglobins (Hbs) with self-association and ligand-binding properties very different from those that characterize the alpha(2)beta(2) tetrameric Hbs of higher vertebrates. Monomeric, ligated
Publikováno v:
The Journal of biological chemistry. 271(47)
The extracellular hemoglobin of the earthworm Lumbricus terrestris has four major kinds of O2-binding chains: a, b, and c (forming a disulfide-linked trimer), and chain d. Non-heme, non-globin structural chains, "linkers," are also present. Light-sca