Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Sidney A. Bernhard"'
Autor:
Sidney A. Bernhard, Peter Tompa
Publikováno v:
Archives of Biochemistry and Biophysics. 276:191-198
Mitochondria were incubated with L[5-13C]glutamic acid and the distribution of the label between the two carboxyl carbon atoms of the L-aspartic acid formed was determined by 13C NMR. The reaction sequence leading from L-glutamic acid to L-aspartic a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf1e7adb5883ae7d5d72de83f3126a1c
https://doi.org/10.1016/0003-9861(90)90026-u
https://doi.org/10.1016/0003-9861(90)90026-u
Autor:
Sidney A. Bernhard, O. P. Malhotra
Publikováno v:
Israel Journal of Chemistry. 12:471-481
The spectra of active-site specific chromophoric acyl enzymes are discussed in terms of both the chemical (electronic) nature of the acyl-enzyme bond and the protein conformation. The evidence presented demonstrates the following: (1) The acyl-enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1848a5bdb8e286ea4d6bf52ab13fc44a
https://doi.org/10.1002/ijch.197400037
https://doi.org/10.1002/ijch.197400037
Autor:
Francois Seydoux, Sidney A. Bernhard
Publikováno v:
Biophysical Chemistry. 1:161-174
The kinetics and stoichiometry of the reaction of sturgeon muscle glyceraldchyde-3-PO 4 -dehydrogenase (GPDH) with the disulfide interchange reagent bis(2,2' dithio-bis(5-nitrobenzoate) (DTNB) has been studied in detail. The native enzyme, a tetramer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::270c01f4ec07f2fc27ff8ce9e5bed665
https://doi.org/10.1016/0301-4622(74)80003-7
https://doi.org/10.1016/0301-4622(74)80003-7
Publikováno v:
Biochemistry. 24:6789-6798
The hydrolysis of beta-(2-furyl)acryloyl phosphate (FAP), catalyzed by the Na+/K+-ATPase, is faster than the catalyzed hydrolysis of ATP. This is due to catalyzed hydrolysis of the pseudosubstrate by K+-dependent states of the enzyme, thus bypassing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d4aaae38e40e6240eddd0b1193bc1821
https://doi.org/10.1021/bi00345a010
https://doi.org/10.1021/bi00345a010
Publikováno v:
Journal of Biological Chemistry. 255:6040-6043
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d0de57b4320429fd3860a93b08cf8ed7
https://doi.org/10.1016/s0021-9258(18)43696-4
https://doi.org/10.1016/s0021-9258(18)43696-4
Autor:
Sidney A. Bernhard
Publikováno v:
Annals of the New York Academy of Sciences. 421:28-40
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::777ee4fb77da09307c4658be74e7658f
https://doi.org/10.1111/j.1749-6632.1983.tb18090.x
https://doi.org/10.1111/j.1749-6632.1983.tb18090.x
Publikováno v:
Journal of Molecular Biology. 108:123-138
Glyceraldehyde 3-phosphate dehydrogenase extracted from sturgeon muscle, exhibits half-site reactivity in its reaction with the pseudo-substrate β -(2-furyl) acryloyl phosphate ( Malhotra & Bernhard, 1968 ). The product is the difurylacryloyl thiol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c47b1a85bb9d627b4c68dc3b17ed6ecd
https://doi.org/10.1016/s0022-2836(76)80099-x
https://doi.org/10.1016/s0022-2836(76)80099-x
Autor:
Sidney A. Bernhard, Jon P. Weber
Publikováno v:
Biochemistry. 21:4189-4194
On the basis of the alternatives of direct inter-enzyme transfer vs. dissociation followed by random diffusion, two kinetic models for metabolite transfer between consecutive enzymes are developed. These two models are readily distinguishable experim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea129b06da9399b4cd6cbb389b25314f
https://doi.org/10.1021/bi00260a042
https://doi.org/10.1021/bi00260a042
Autor:
Sidney A. Bernhard
Publikováno v:
Cell Biophysics. 12:119-132
A new model for the organization and flow of metabolites through a metabolic pathway is presented. The model is based on four major findings. (1) The intracellular concentrations of enzyme sites exceed the concentrations of intermediary metabolites t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64972eaa706414a13f86ab0c4813768a
https://doi.org/10.1007/bf02918354
https://doi.org/10.1007/bf02918354
Publikováno v:
Biochimie. 63:131-141
Summary A variety of species of GPDH undergo acylation at two of the four active cystein sites per mole of tetrameric enzyme. This reaction requires tightly bound NAD + , a situation restricted to two of the four NAD sites per tetramer. S → N acyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2450f959725dca551c20e4326d0f5e8f
https://doi.org/10.1016/s0300-9084(81)80177-0
https://doi.org/10.1016/s0300-9084(81)80177-0