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Preparation of an Active Soluble Lactate Dehydrogenase-Nicotinamide Adenine Dinucleotide Complex Using Glutaraldehyde

Venn, R. F. ; Larsson, P. O. LU and Mosbach, K. LU (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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publishing date
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}},
}