Zobrazeno 1 - 8
of 8
pro vyhledávání: '"G D McClure"'
Publikováno v:
Radiation Effects and Defects in Solids. 135:217-221
Laser selective excitation is used to study the spectroscopic properties of Er3+ ions doped in Lithium Niobate (LNB) single crystals, where it substitutes for the Li+ or Nb5+ sites both having local C3 symmetry. Excited state absorption resulting in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::93bce3523d53c2f20baf449431fc932c
https://doi.org/10.1080/10420159508229839
https://doi.org/10.1080/10420159508229839
Publikováno v:
Journal of Biological Chemistry. 267:23596-23600
The enzyme rhodanese (thiosulfate sulfurtransferase, EC 2.8.1.1) is inactivated on incubation with reducing sugars such as glucose, mannose, or fructose, but is stable with non-reducing sugars or related polyhydroxy compounds. The enzyme is inactivat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7d48d92eea28e837bb4fe4dd9af0e62f
https://doi.org/10.1016/s0021-9258(18)35880-0
https://doi.org/10.1016/s0021-9258(18)35880-0
Publikováno v:
International Archives of Allergy and Immunology. 107:69-71
Partially purified commercial phospholipase D (PLD) was fractionated by dye-ligand affinity chromatography and nondenaturing polyacrylamide gel electrophoresis (PAGE). Active material migrated as three bands on SDS-PAGE. The two higher-abundance spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::513e78e1b4cd0a08ec431af9f49a8514
https://doi.org/10.1159/000236934
https://doi.org/10.1159/000236934
Publikováno v:
International archives of allergy and immunology. 107(1-3)
Partially purified commercial phospholipase D (PLD) was fractionated by dye-ligand affinity chromatography and nondenaturing polyacrylamide gel electrophoresis (PAGE). Active material migrated as three bands on SDS-PAGE. The two higher-abundance spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dff11dd80e7a6dfa44ae98267816b584
https://pubmed.ncbi.nlm.nih.gov/7613220
https://pubmed.ncbi.nlm.nih.gov/7613220
Publikováno v:
Biochemistry. 32(7)
Theory for enzyme-catalyzed reactions is developed for the dependence on product concentration of deuterium isotope effects on V and V/K. Generally, a product that decreases the off-rate for a second product to zero causes the isotope effect on V/K t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::819a5e217823c962701bb0f01599260e
https://pubmed.ncbi.nlm.nih.gov/8439540
https://pubmed.ncbi.nlm.nih.gov/8439540
Publikováno v:
Journal of enzyme inhibition. 7(2)
A method has been developed for counting active sites of cyclic-AMP-dependent protein kinase. Known concentrations of a synthetic peptide similar to a fragment of the endogenous inhibitor of the kinase were included in otherwise routine assay mixes c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b5ef850911e4dd8438ddbe3b7cdbccd
https://pubmed.ncbi.nlm.nih.gov/7509870
https://pubmed.ncbi.nlm.nih.gov/7509870
Publikováno v:
The Journal of biological chemistry. 267(33)
The enzyme rhodanese (thiosulfate sulfurtransferase, EC 2.8.1.1) is inactivated on incubation with reducing sugars such as glucose, mannose, or fructose, but is stable with non-reducing sugars or related polyhydroxy compounds. The enzyme is inactivat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f5b7b7b27a07ad5e79adad2b412cdcfc
https://pubmed.ncbi.nlm.nih.gov/1429701
https://pubmed.ncbi.nlm.nih.gov/1429701
Publikováno v:
Journal of toxicology and environmental health. 31(2)
Effects of trifluoroacetic acid (TFA) on cell growth, DNA, glycoprotein, and dolichol-linked oligosaccharides synthesis and ribonucleotide triphosphate concentrations were examined in exponentially growing C6 murine glioma cells. One day of treatment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55185994b5bf1f4e1116cbc0809b7cbb
https://pubmed.ncbi.nlm.nih.gov/2213926
https://pubmed.ncbi.nlm.nih.gov/2213926