Zobrazeno 1 - 10
of 45
pro vyhledávání: '"S M, Schuster"'
Autor:
C M, Westhoff, O, Lopez, P, Goebel, L, Carlson, R R, Carlson, F W, Wagner, S M, Schuster, D E, Wylie
Publikováno v:
Proteins. 37(3)
Monoclonal antibodies (mAb) specific for mercuric ions were isolated from BALB/c mice injected with a mercury-containing, hapten-carrier complex. The antibodies reacted by enzyme-linked immunosorbent assay with bovine serum albumin-glutathione-mercur
Publikováno v:
The Biochemical journal. 339
Transcription of the asparagine synthetase (AS) gene is induced by amino acid deprivation. The present data illustrate that this gene is also under transcriptional control by carbohydrate availability. Incubation of human HepG2 hepatoma cells in gluc
Autor:
N G, Richards, S M, Schuster
Publikováno v:
Advances in enzymology and related areas of molecular biology. 72
The enzymatic synthesis of asparagine is an ATP-dependent process that utilizes the nitrogen atom derived from either glutamine or ammonia. Despite a long history of kinetic and mechanistic investigation, there is no universally accepted catalytic me
Publikováno v:
The Journal of biological chemistry. 269(43)
Although Arg-30, Asn-74, and Asn-79 appear totally conserved throughout the purF glutamine-dependent amidotransferases, their potential roles in catalysis and binding remain unexplored for any member of the enzyme family. Here we report the overexpre
Publikováno v:
The Journal of biological chemistry. 269(10)
The mechanism of nitrogen transfer in glutamine-dependent amidotransferases remains to be unambiguously established. We now report the overexpression, purification, and kinetic characterization of both the glutamine- and ammonia-dependent activities
Publikováno v:
The Journal of biological chemistry. 268(22)
Cys-1 mutants of recombinant human asparagine synthetase were constructed and their ability to catalyze the glutamine-dependent nitrogen transfer reaction required for asparagine biosynthesis was determined. In agreement with previous work, altering
Autor:
S, Sheng, S M, Schuster
Publikováno v:
The Journal of biological chemistry. 268(7)
A yeast protein was purified from wild type Saccharomyces cerevisiae (S. cerevisiae) to near homogeneity using an ethanolamine affinity chromatography procedure. The N-terminal amino acid sequencing and the amino acid composition analyses identified
Publikováno v:
The Journal of biological chemistry. 268(2)
The resistance of certain tumor cells to the chemotherapeutic agent L-asparaginase has often been found to be associated with the presence of asparagine synthetase activity. In an attempt to study the translational regulation of the asparagine synthe
Autor:
S, Sheng, S M, Schuster
Publikováno v:
BioTechniques. 13(5)
Publikováno v:
The Journal of biological chemistry. 267(1)
A highly conserved protein motif characteristic of Class II aminoacyl tRNA synthetases was found to align with a region of Escherichia coli asparagine synthetase A. The alignment was most striking for aspartyl tRNA synthetase, an enzyme with catalyti