Zobrazeno 1 - 7
of 7
pro vyhledávání: '"F. L. Boyd"'
Autor:
F. L. Boyd, K. J. Alexy, D. I. Hall, Karl V. Miller, J. W. Gassett, T. H. Folk, B. R. Chapman
Publikováno v:
The Wilson Bulletin. 112:268-271
Cattle Egrets (Bubulcus ibis) expanded their range greatly during the twentiethth century, making localized food habit studies necessary to determine their impact in newly invaded ecosystems. We examined 44 Cattle Egret stomachs collected in January
Publikováno v:
Journal of the American Chemical Society. 112:3279-3289
Publikováno v:
The Journal of biological chemistry. 267(35)
beta-L-3'-Deoxythymidine 5'-triphosphate (L-ddTTP) and beta-L-3'-deoxy-2',3'-didehydrothymidine 5'-triphosphate (L-d4TTP) were substrates for human immunodeficiency virus reverse transcriptase, Escherichia coli DNA polymerase I (Klenow), and Sequenas
Publikováno v:
The Journal of biological chemistry. 267(29)
Two enantiomers of carbovir, a carbocyclic analog of 2',3'-dideoxyguanosine, were compared with respect to their phosphorylation and the phosphorylation of their nucleotides by mammalian enzymes. 5'-Nucleotidase catalyzed the phosphorylation of (-)-c
Autor:
D J, Porter, F L, Boyd
Publikováno v:
The Journal of biological chemistry. 267(5)
S-Adenosylhomocysteine hydrolase (SAHase) was resolved into apoenzyme and NAD+ by acidic ammonium sulfate treatment. The apoenzyme was catalytically inactive, but could be reconstituted to active enzyme with NAD+. Reduced SAHase (ENADH) that was prep
Autor:
D J, Porter, F L, Boyd
Publikováno v:
The Journal of biological chemistry. 266(32)
The kinetic mechanism of S-adenosylhomocysteine hydrolase was investigated by stopped-flow spectrofluorometry at pH 7.0 and 25 degrees C. Pre-steady-state kinetic steps were identified with chemical steps proposed for the mechanism of this enzyme (Pa
Publikováno v:
Nucleosides and Nucleotides. 2:479-494
Glycosylation of the heterocycle, 6,7-dihydro-imidazo [4,5-d] [1,3] diazepin-8(3H)-one, with suitably protected sugars under the influence of Lewis acid catalysts gave the β-D-ribo- and 3′-deoxy-β-D-erythropento-furanosyl nucleosides. Deprotectio