Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Claudia T. Evans"'
Publikováno v:
Hereditas. 117:39-43
Citrate synthase (CS) is a key enzyme of the Krebs tricarboxylic acid cycle. A 1.4 kb porcine CS cDNA probe was used to chromosomally localize the CS gene in pigs by in situ hybridization. Two in situ hybridization experiments were conducted. Althoug
Publikováno v:
Biochemistry. 35:10661-10672
We examined the catalytic efficiency of 18 pig citrate synthase mutants. The residues mutated were selected according to two criteria: the conservation of that residue in all known citrate synthase sequences, and the importance of that residue in sub
Autor:
Christer Lindbladh, Klaus Mosbach, C Hagglund, M Rault, W. C. Small, Paul A. Srere, Leif Bülow, Claudia T. Evans
Publikováno v:
Biochemistry. 33:11692-11698
We have expressed the DNA of the fusion of CS1 to MDH1 in Escherichia coli gltA-. The fusion protein (CS1/MDH1) is the C-terminus of CS1 linked in-frame to the N-terminus of MDH1 with a short linker of glycyl-seryl-glycyl. The fusion protein produced
Autor:
Saba E. Demian, Stuart I. Myers, Claudia T. Evans, Barbara Kalley-Taylor, L. Bartula, Angela Riva, Lindsey Inman
Publikováno v:
Molecular and Cellular Endocrinology. 95:129-138
Gallbladder explants from control rabbits and rabbits subjected to bile duct ligation (BDL) for 24 and 72 h (cholecystitis model) were placed in cell culture to determine the source for increased gallbladder prostanoid synthesis during cholecystitis.
Publikováno v:
Biochemistry. 31:7908-7914
Acetyl-CoA enol has been proposed as an intermediate in the citrate synthase (CS) reaction with Asp375 acting as a base, removing a proton from the methyl carbon of acetyl-CoA, and His274 acting as an acid, donating a proton to the carbonyl [Karpusas
Publikováno v:
Biochemistry. 30:9281-9286
The conformational stabilities of native pig citrate synthase (PCS), a recombinant wild-type PCS, and six active-site mutant pig citrate synthases were studied in thermal denaturation experiments by circular dichroism and in urea denaturation experim
Autor:
Daniel W. Foster, Clive A. Slaughter, Claudia T. Evans, Victoria Esser, J. D. McGarry, N. F. Brown, A D Gonzalez
Publikováno v:
Journal of Biological Chemistry. 266:15446-15449
[35S]Methionine-labeled porcine heart citrate synthase (used here as a positive control) and rat liver carnitine palmitoyltransferase II (CPT II) were generated by in vitro transcription and translation of their cDNA constructs in appropriate Bluescr
Publikováno v:
Biochemistry. 29:7557-7563
Two amino acid residues, His274 and Asp375, were replaced singly in the active site of pig citrate synthase (PCS) with Gly274, Arg274, Gly375, Asn375, Glu375, and Gln375. The nonmutant protein and the mutant proteins were expressed in and purified fr
Autor:
Claudia T. Evans, Michael E. Ullian, Joel Z. Melnick, Wayne R. Fitzgibbon, Christopher J. Robinson
Publikováno v:
Hypertension (Dallas, Tex. : 1979). 35(4)
Abstract —Aldosterone and other mineralocorticoids increase citrate synthase activity in the kidney and enhance renal sodium reabsorption, but it is unclear whether the increased citrate synthase activity is involved in renal sodium transport. We u
Publikováno v:
Molecular and cellular endocrinology. 115(1)
Gallbladder cell cultures obtained from rabbits subjected to sham or 72 h of bile duct ligation (72 h BDL, cholecystitis model) were incubated with calcium ionophore (A23187), dibutyryl cAMP (cAMP), and phorbol 12,13-diacetate (phorbol) to determine