Zobrazeno 1 - 10
of 60
pro vyhledávání: '"J E, Churchich"'
Publikováno v:
Journal of Biological Chemistry. 267:15032-15040
Bacteriophage T7 gene 2.5 protein has been shown to interact with T7 DNA polymerase (the complex of T7 gene 5 protein and Escherichia coli thioredoxin) by affinity chromatography and fluorescence emission anisotropy. T7 DNA polymerase binds specifica
Autor:
P Y, Cheung, J E, Churchich
Publikováno v:
The Journal of biological chemistry. 274(46)
Refolding of partially folded mitochondrial malate dehydrogenase (mMDH) is assisted by protein-disulfide isomerase (PDI). The addition of a 20-fold molar excess of PDI over denatured protein (0. 1 microM) accelerates the recovery of catalytic activit
Publikováno v:
The international journal of biochemistrycell biology. 30(12)
Porcine brain pyridoxal kinase has been cloned. A 1.2 kilo-based cDNA with a 966-base pair open reading frame was determined from a porcine brain cortex cDNA library using PCR technique. The DNA sequence was shown to encode a protein of 322 amino aci
Autor:
J E, Churchich
Publikováno v:
The Journal of biological chemistry. 272(32)
2'-Deoxy-3'-anthraniloyl adenosine-5-triphosphate (ANT-dATP) coordinated to Tb3+ was used as an environmentally sensitive probe of the nucleotide-binding site of GroEL. Tb3+.ANT-dATP recognizes the nucleotide-binding site of GroEL and inhibits ATPase
Publikováno v:
Biochemistry and molecular biology international. 38(4)
Several spectroscopic methods have been used to study the structure of beta-lactoglobulin B at pH 2.1 in the presence of 8M urea. Fluorescence and polarization of fluorescence spectroscopy measurements indicate that the two tryptophanyl residues of t
Publikováno v:
Archives of biochemistry and biophysics. 313(2)
In the presence of myo -inositol monophosphatase, terbium ions can be excited by energy transfer from the aromatic side chains of the protein. This enhancement of Tb 3+ luminescence due to its binding to the enzyme at pH 6.5 was used to determine the
Publikováno v:
Biochemistry and molecular biology international. 32(2)
Reversible dissociation of the dimeric structure of brain myo-inositol monophosphatase into subunits was attained by the addition of guanidine-HCl (4M). The molecular mass of the subunits (29 KDa) was determined by HPLC chromatography. Separation of
Autor:
O S, Kwon, J E, Churchich
Publikováno v:
The Journal of biological chemistry. 269(1)
Fluorescence techniques have been used to investigate the interaction of bovine 70-kDa heat shock cognate protein (Hsc 70) with small molecular weight peptides and myo-inositol monophosphatase. The emission properties of Hsc 70 remain invariant upon
Autor:
T, Pineda, J E, Churchich
Publikováno v:
The Journal of biological chemistry. 268(27)
The unfolding of brain pyridoxal kinase by guanidinium HCl has been investigated at equilibrium. The overall process was reversible as judged from the complete recovery of catalytic activity after removal of guanidinium HCl. Unfolding of pyridoxal ki
Publikováno v:
The Journal of biological chemistry. 268(11)
myo-Inositol monophosphatase isolated from pig brain is a very stable dimeric protein characterized by a rotational correlation time of 30 ns. The unfolding and dissociation of the dimeric enzyme (58 kDa) by guanidine hydrochloride have been investig