Zobrazeno 1 - 10
of 49
pro vyhledávání: '"R W, Gracy"'
Publikováno v:
Proteomics. 1(3)
Chemiluminescent probes offer highly sensitive quantitative analyses of proteins blotted from electrophoretic gels onto a supporting matrix (e.g. nitrocellulose or polyvinylidene difluoride). Visualization of signals from probes involves the emission
Publikováno v:
Proteomics. 1(7)
The oxidative modification of proteins plays a major role in a number of human diseases, but identity of the specific proteins that are most susceptible to oxidation has posed a difficult problem. Protein carbonyls are increased after oxidative stres
Publikováno v:
The Journal of the American Osteopathic Association. 101(6)
Many patients with arthritis are using alternative modes of therapy, including nutritional supplements, to treat their arthritis. Most patients never tell their doctors that they are taking alternative medications, and few doctors even ask about such
Publikováno v:
The Journal of experimental zoology. 282(1-2)
Our studies focus on the mechanisms of molecular wear and tear, terminal marking, protein degradation, and how these processes are altered with age. Molecular wear and tear directly links catalysis with postsynthetic terminal marking. For example, th
Publikováno v:
Archives of biochemistry and biophysics. 317(1)
Triosephosphate isomerase (TPI) provides an excellent model for terminal marking and protein degradation. Mammalian TPI is terminally modified by deamidation at Asn71-Gly, resulting in unfolding, dissociation, and proteolysis. In contrast, chicken TP
Publikováno v:
The Journal of biological chemistry. 269(7)
Covalent modification of Glu165 in the catalytic center of triose-phosphate isomerase with the substrate analogue 3-chloroacetol phosphate traps the complex in two conformations. The two resulting 31P NMR resonances at 6.9 and 5.7 ppm appear to refle
Publikováno v:
The Journal of biological chemistry. 268(36)
Limited proteolysis of the triose-phosphate isomerase (EC 5.3.1.1) by subtilisin generates peptides that remain noncovalently attached and catalytically active. Edman degradation of the peptides showed that the primary proteolytic sites for yeast tri
Publikováno v:
The Journal of biological chemistry. 267(28)
The effects of unfolding, refolding, and hybridization of triosephosphate isomerase (TPI) subunits from different species and subunits which have been specifically modified at the active site have been examined. These effects have been evaluated in t
Publikováno v:
Progress in clinical and biological research. 344
Publikováno v:
Progress in clinical and biological research. 358