Activity of select dehydrogenases with Sepharose-immobilized N6-carboxymethyl-NAD
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Activity of select dehydrogenases with Sepharose-immobilized N6-carboxymethyl-NAD
N(6)-carboxymethyl-NAD (N(6)-CM-NAD) can be used to immobilize NAD onto a substrate containing terminal primary amines. We previously immobilized N(6)-CM-NAD onto sepharose beads and showed that Thermotoga maritima glycerol dehydrogenase could use the immobilized cofactor with cofactor recycling. We now show that Saccharomyces cerevisiae alcohol dehydrogenase, rabbit muscle L-lactate dehydrogen...
متن کاملReversible cross-linking of alcohol and lactate dehydrogenases with the bifunctional reagent N2,N'2-adipodihydrazido-bis-(N6-carboxymethyl-NAD+)
Affinity precipitation with N,, N,'-adipodihydrazido-bis( N6-carboxymethyl-NAD+) (bis-NAD+) as a means of isolating alcohol dehydrogenase (EC 1.1.1.1) and lactate dehydrogenase (EC 1.1.1.27) has already been reported (Flygare et al., 1983; Beattie et al., 1984). However, affinity precipitation of alcohol dehydrogenase in the presence of bis-NAD+ and pyrazole has been found to give mixed results...
متن کاملThe selective retardation of NADP+-dependent dehydrogenases by immobilized procion red HE-3B.
The capacities of Procion Red HE-3B and Cibacron Blue F3G-A immobilized to Sepharose CL-4B and Matrex 201R for NAD+-, NADP+- and NAD(P)+-dependent dehydrogenases were measured. Procion Red HE-3B columns retarded NADP+-dependent dehydrogenases more effectively than NAD+-dependent dehydrogenases, whilst immobilized Cibacron Blue F3G-A retarded NAD+-dependent dehydrogenases more effectively than N...
متن کاملMycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors
During human infection, Mycobacterium tuberculosis (Mtb) survives the normally bacteriocidal phagosome of macrophages. Mtb and related species may be able to combat this harsh acidic environment which contains reactive oxygen species due to the mycobacterial genomes encoding a large number of dehydrogenases. Typically, dehydrogenase cofactor binding sites are open to solvent, which allows NAD/N...
متن کاملInhibition studies of dehydrogenases by structural analogues of NAD.
The coenzyme anologues [3-(2-acetylpyridinio) propyl]-adenosine pyrophosphate and [3-(2-bromoacetylpyridinio) -propyl] -adenosine pyrophoshate were synthesized and used for inhibition studies. While the first compound reacts as competitive inhi bitor against NAD+, the latter is able to form co valently bound derivatives of several NAD+-dependent dehydrogenases, giving informations about amino...
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ژورنال
عنوان ژورنال: Bioengineered
سال: 2015
ISSN: 2165-5979,2165-5987
DOI: 10.1080/21655979.2014.1004020