Preparation of an Active Soluble Lactate Dehydrogenase-Nicotinamide Adenine Dinucleotide Complex Using Glutaraldehyde
(1977) In Acta Chemica Scandinavica 31b. p.141-144- Abstract
- The cofactor analogue N6-((6-aminohexyl)-carbamoylmethyl)-NAD was bound to beef heart lactate dehydrogenase by the glutaraldehyde coupling method and the enzyme-coenzyme complex subsequently separated from excess of non-coupled cofactor by gel filtration chromatography. The number of cofactor molecules bound per enzyme molecule could be varied between 0 and 8 by altering the coupling time. The enzyme-coenzyme preparation could catalyze the reaction lactate to pyrovate in the absence of externally added cofactor although with low efficiency. The enzyme-coenzyme preparation was also immobilized on Sepharose in such a way that possible contact between complexes was minimized (low substitution of the gel) and the activity of the... (More)
- The cofactor analogue N6-((6-aminohexyl)-carbamoylmethyl)-NAD was bound to beef heart lactate dehydrogenase by the glutaraldehyde coupling method and the enzyme-coenzyme complex subsequently separated from excess of non-coupled cofactor by gel filtration chromatography. The number of cofactor molecules bound per enzyme molecule could be varied between 0 and 8 by altering the coupling time. The enzyme-coenzyme preparation could catalyze the reaction lactate to pyrovate in the absence of externally added cofactor although with low efficiency. The enzyme-coenzyme preparation was also immobilized on Sepharose in such a way that possible contact between complexes was minimized (low substitution of the gel) and the activity of the immobilised complex was foound to be partly retained, indicating that a cofactor molecule can inteact with the enzyme molecule to which it is bound. (Less)
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https://lup.lub.lu.se/record/b6f29242-20c8-42d0-8634-18381d524d69
- author
- Venn, R. F. ; Larsson, P. O. LU and Mosbach, K. LU
- organization
- publishing date
- 1977
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Acta Chemica Scandinavica
- volume
- 31b
- pages
- 4 pages
- publisher
- Munksgaard Forlag
- ISSN
- 0001-5393
- DOI
- 10.3891/acta.chem.scand.31b-0141
- language
- English
- LU publication?
- yes
- id
- b6f29242-20c8-42d0-8634-18381d524d69
- date added to LUP
- 2024-06-22 16:04:42
- date last changed
- 2024-09-13 11:15:30
@article{b6f29242-20c8-42d0-8634-18381d524d69, abstract = {{The cofactor analogue N<sup>6</sup>-((6-aminohexyl)-carbamoylmethyl)-NAD was bound to beef heart lactate dehydrogenase by the glutaraldehyde coupling method and the enzyme-coenzyme complex subsequently separated from excess of non-coupled cofactor by gel filtration chromatography. The number of cofactor molecules bound per enzyme molecule could be varied between 0 and 8 by altering the coupling time. The enzyme-coenzyme preparation could catalyze the reaction lactate to pyrovate in the absence of externally added cofactor although with low efficiency. The enzyme-coenzyme preparation was also immobilized on Sepharose in such a way that possible contact between complexes was minimized (low substitution of the gel) and the activity of the immobilised complex was foound to be partly retained, indicating that a cofactor molecule can inteact with the enzyme molecule to which it is bound.}}, author = {{Venn, R. F. and Larsson, P. O. and Mosbach, K.}}, issn = {{0001-5393}}, language = {{eng}}, pages = {{141--144}}, publisher = {{Munksgaard Forlag}}, series = {{Acta Chemica Scandinavica}}, title = {{Preparation of an Active Soluble Lactate Dehydrogenase-Nicotinamide Adenine Dinucleotide Complex Using Glutaraldehyde}}, url = {{http://dx.doi.org/10.3891/acta.chem.scand.31b-0141}}, doi = {{10.3891/acta.chem.scand.31b-0141}}, volume = {{31b}}, year = {{1977}}, }