Zobrazeno 1 - 10
of 12
pro vyhledávání: '"D J Opheim"'
Autor:
R W Bernlohr, D J Opheim
Publikováno v:
Journal of Biological Chemistry. 250:3024-3033
The fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) from the spore-forming bacterium Bacillus licheniformis was purified approximately 800-fold (with a 20% yield of activity) by a procedure that included ammo
Autor:
D J Opheim, O Touster
Publikováno v:
Journal of Biological Chemistry. 253:1017-1023
Rat liver contains alpha-D-mannosidases in lysosomes, Golgi membranes, and cytosol. The lysosomal enzyme has now been purified approximately 30,000-fold over the crude extract and is free of at least 13 other lysosomal hydrolases. The enzyme has an a
Publikováno v:
Journal of Biological Chemistry. 252:3227-3233
Autor:
O Touster, D J Opheim
Publikováno v:
Journal of Biological Chemistry. 252:739-743
The alpha-L-fucosidase from rat liver lysosomes was purified approximately 27,000-fold (from cytoplasmic extract) by a rapid procedure requiring only 7 h anf providing enzyme in a 20 per cent yield. The procedure is based upon affinity chromatography
Autor:
D J, Opheim, R W, Bernlohr
Publikováno v:
Methods in enzymology.
Autor:
D J Opheim, S Berardinelli
Publikováno v:
Journal of clinical microbiology. 22(5)
A new germ tube induction medium, composed of three parts Rabbit Coagulase Plasma with EDTA (BBL Microbiology Systems) and two parts Tryp-Soy broth (Scott Laboratories, Inc.), was effective for the presumptive identification of Candida albicans. This
Autor:
D J, Opheim, R W, Bernlohr
Publikováno v:
The Journal of biological chemistry. 250(8)
The fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) from the spore-forming bacterium Bacillus licheniformis was purified approximately 800-fold (with a 20% yield of activity) by a procedure that included ammo
Autor:
D J, Opheim, O, Touster
Publikováno v:
The Journal of biological chemistry. 253(4)
Rat liver contains alpha-D-mannosidases in lysosomes, Golgi membranes, and cytosol. The lysosomal enzyme has now been purified approximately 30,000-fold over the crude extract and is free of at least 13 other lysosomal hydrolases. The enzyme has an a
Autor:
D J, Opheim, O, Touster
Publikováno v:
Methods in enzymology. 50
Publikováno v:
The Journal of biological chemistry. 252(10)