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Affinity precipitation of dehydrogenases

Flygare, Susanne ; Griffin, Tadhg ; Larsson, Per-Olof LU and Mosbach, Klaus LU (1983) In Analytical Biochemistry 133(2). p.409-416
Abstract
Affinity precipitation, a novel technique closely related to immunoprecipitation and affinity chromatography, has been evaluated in systems comprised of dehydrogenases and a bifunctional NAD derivative, Bis-NAD. Lactate dehydrogenase and glutamate dehydrogenase were easily precipitated whereas yeast alcohol dehydrogenase required the presence of salt to enhance the affinity precipitation. Liver alcohol dehydrogenase did not precipitate, probably because most of the affinity complexes formed were composed of only two enzyme molecules. Affinity precipitation was carried out on a preparative scale for the isolation of ox heart lactate dehydrogenase from a crude extract. The yield and purity of the enzyme and the general properties of the... (More)
Affinity precipitation, a novel technique closely related to immunoprecipitation and affinity chromatography, has been evaluated in systems comprised of dehydrogenases and a bifunctional NAD derivative, Bis-NAD. Lactate dehydrogenase and glutamate dehydrogenase were easily precipitated whereas yeast alcohol dehydrogenase required the presence of salt to enhance the affinity precipitation. Liver alcohol dehydrogenase did not precipitate, probably because most of the affinity complexes formed were composed of only two enzyme molecules. Affinity precipitation was carried out on a preparative scale for the isolation of ox heart lactate dehydrogenase from a crude extract. The yield and purity of the enzyme and the general properties of the procedure are considered very satisfactory. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Affinity precipitation, Bis-NAD, LDG, GDH, Liver ADH, Yeast ADH
in
Analytical Biochemistry
volume
133
issue
2
pages
8 pages
publisher
Elsevier
external identifiers
  • scopus:0020825575
ISSN
0003-2697
DOI
10.1016/0003-2697(83)90102-1
language
English
LU publication?
yes
id
07188120-05e1-4dd0-a8c3-8870f32057d7
date added to LUP
2024-06-18 15:21:30
date last changed
2024-09-06 12:49:02
@article{07188120-05e1-4dd0-a8c3-8870f32057d7,
  abstract     = {{Affinity precipitation, a novel technique closely related to immunoprecipitation and affinity chromatography, has been evaluated in systems comprised of dehydrogenases and a bifunctional NAD derivative, Bis-NAD. Lactate dehydrogenase and glutamate dehydrogenase were easily precipitated whereas yeast alcohol dehydrogenase required the presence of salt to enhance the affinity precipitation. Liver alcohol dehydrogenase did not precipitate, probably because most of the affinity complexes formed were composed of only two enzyme molecules. Affinity precipitation was carried out on a preparative scale for the isolation of ox heart lactate dehydrogenase from a crude extract. The yield and purity of the enzyme and the general properties of the procedure are considered very satisfactory.}},
  author       = {{Flygare, Susanne and Griffin, Tadhg and Larsson, Per-Olof and Mosbach, Klaus}},
  issn         = {{0003-2697}},
  keywords     = {{Affinity precipitation; Bis-NAD; LDG; GDH; Liver ADH; Yeast ADH}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{409--416}},
  publisher    = {{Elsevier}},
  series       = {{Analytical Biochemistry}},
  title        = {{Affinity precipitation of dehydrogenases}},
  url          = {{http://dx.doi.org/10.1016/0003-2697(83)90102-1}},
  doi          = {{10.1016/0003-2697(83)90102-1}},
  volume       = {{133}},
  year         = {{1983}},
}