Zobrazeno 1 - 10
of 21
pro vyhledávání: '"H. Olin Spivey"'
Autor:
H. Olin Spivey, Zeljko M Svedruzić
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 63:501-511
The exceptionally high protein concentration in living cells can favor functional protein-protein interactions that can be difficult to detect with purified proteins. In this study we describe specific interactions between mammalian D-glyceraldehyde-
Publikováno v:
Langmuir. 20:8307-8312
Four different quaternary ammonium chloride-modified poly(propylenimine) (PPI) dendrimers were synthesized by alkylation of a PPI dendrimer having eight dimethylamino end groups with 1-bromooctane or 1-bromododecane. By varying the mole ratio of alky
Publikováno v:
Biochemistry. 42:6259-6263
Evidence for the NADH-modulated formation of a complex between alpha-glycerol-3-phosphate dehydrogenase and l-lactate dehydrogenase was reported [Yong, H., Thomas, G. A., and Peticolas, W. L. (1993) Biochemistry 32, 11124-11131]. This NADH-modulated
Autor:
H. Olin Spivey, Kimberly A. Vonnahme, Rodney D. Geisert, Stephen P. Ford, Jerry R. Malayer, A. C. Clutter
Publikováno v:
Biology of Reproduction. 61:1235-1241
Porcine conceptuses rapidly elongate within the uterine horns prior to the period of placental attachment. During the time of elongation, secretion of estrogen by the developing conceptuses occurs for the establishment of pregnancy through maintenanc
Publikováno v:
Analytical Biochemistry. 253:190-195
We present an enzymatic method for the determination of l -[ 14 C]lactate specific radioactivity in complex biological samples containing other radiolabeled compounds. The method is based on the conversion of l -lactate to l -pyruvate by lactate oxid
Publikováno v:
Analytical biochemistry. 334(2)
A method for the quantitative assay of mammalian cell micropermeabilization is described. The method is based on the permeabilization-induced loss of endogenous glycolytic cofactors and consequent discontinuation of cellular lactate production. Advan
Publikováno v:
Journal of molecular recognition : JMR. 7(4)
As previously reported, mitochondrial malate dehydrogenase (MDH) binds to purified complex I of the electron transport system. With conditions used in previous reports, MDH binds even more extensively, but probably predominantly non-specifically, to
Publisher Summary This chapter discusses substrate channeling of NADH in mitochondrial redox processes. With purified complex I, even low levels of NAD or NADH decreased its associations with most dehydrogenases to below detectable limits. Therefore,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef1ece045a2bb1757852b1d16fb614a6
https://doi.org/10.1016/b978-0-12-152833-1.50022-8
https://doi.org/10.1016/b978-0-12-152833-1.50022-8
Publikováno v:
Archives of Biochemistry and Biophysics. 205:380-387
The kinetic data of Bryce et al. [ C. F. A. Bryce, D. C. Williams, R. A. John, and P. Fasella (1976) , Biochem. J. , 153 , 571–577] indicated anomalous behavior of the coupled aspartate aminotransferase and malate dehydrogenase reactions. From meas
Autor:
H. Olin Spivey, Karen S. McGurk
Publikováno v:
Biochemical Journal. 177:697-705
Apparent conformational transitions induced in chicken liver pyruvate carboxylase by substrates, KHCO3 and MgATP, and the allosteric effector, acetyl-CoA, were studied by using the fluorescent probe, 8-anilinonaphthalene-1-sulphonic acid and c.d. Flu