Affinity precipitation of dehydrogenases
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/07188120-05e1-4dd0-a8c3-8870f32057d7
- author
- Flygare, Susanne ; Griffin, Tadhg ; Larsson, Per-Olof LU and Mosbach, Klaus LU
- organization
- publishing date
- 1983
- 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}}, }