Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Chaomei Lin"'
Publikováno v:
Journal of Biological Chemistry. 274:9648-9655
We previously raised an antibody (RA6.3) by an antiidiotypic approach which was designed to be directed against an amiloride binding domain on the epithelial Na+ channel (ENaC). This antibody mimicked amiloride in that it inhibited transepithelial Na
Autor:
Chaomei Lin, Catherine M. Fuller, Roger T. Worrell, Douglas C. Eaton, Holly K. Patton, Vadim Shlyonsky, Weijing Sun, Bakhram K. Berdiev, Jonathan B. Zuckerman, Thomas R. Kleyman, Dale J. Benos, Iskander I. Ismailov, Thomas Kieber-Emmons
Publikováno v:
Journal of Biological Chemistry. 272:21075-21083
Limited information is available regarding domains within the epithelial Na+ channel (ENaC) which participate in amiloride binding. We previously utilized the anti-amiloride antibody (BA7.1) as a surrogate amiloride receptor to delineate amino acid r
Autor:
Farhad Kosari, Thomas R. Kleyman, Chaomei Lin, Thomas Kieber-Emmons, Katherine V. Prammer, Annabelle Villalobos
Publikováno v:
Kidney International. 48:956-964
Defining topological similarities among ion transport proteins with anti-amiloride antibodies. The structural features of amiloride binding sites on amiloride-sensitive transport proteins have received limited characterization. An antibody that recog
Publikováno v:
Journal of Pharmacy and Pharmacology. 43:200-203
Rats were implanted subcutaneously with osmotic mini-pumps containing either 0.9% NaCl, nicotine (1.5 or 4.5 mg kg−1 day−1), or cocaine (30 mg kg−1 day−1), for 14 days. Neither nicotine nor cocaine treatment significantly altered the maximal
Publikováno v:
American journal of physiology. Renal physiology. 285(6)
One of the defining characteristics of the epithelial sodium channel (ENaC) is its block by the diuretic amiloride. This study investigates the role of the extracellular loop of the α-subunit of ENaC in amiloride binding and stabilization. Mutations
Publikováno v:
The American journal of physiology. 267(3 Pt 1)
Amiloride and related compounds have found widespread use as cation transport inhibitors. We have previously raised a series of polyclonal anti-amiloride antibodies using different amiloride-protein conjugates as immunogens, where amiloride was coupl
Publikováno v:
Analytical biochemistry. 198(1)
125I-containing compounds that react specifically with sulfhydryl groups were prepared in yields of 30 to 40% on the basis of starting 125I quantity. The synthetic precursors were commercially available heterobifunctional crosslinkers and the peptide
Publikováno v:
Biochemical pharmacology. 41(5)
The antagonist potency of a series of bivalent adrenocorticotropic hormone (ACTH) peptides was examined using suspensions of inner zone rat adrenocortical cells. Bivalent antagonists were prepared by bis(maleimide) covalent cross-linking of carboxyl
Publikováno v:
Biochimica et biophysica acta. 1038(3)
A two-step procedure for introduction of sulfhydryl groups at protein carboxyl groups is described. The resultant proteins contain 2-aminoethanethiol residues bound by amide linkages to the protein carboxyl groups. First an amide bond is formed betwe
Publikováno v:
American Journal of Physiology: Cell Physiology; Sep1994, Vol. 267 Issue 3, pC821-C826, 6p