Literature DB >> 218564

The preparation of stable enzyme-coenzyme complexes with endogenous catalytic activity.

P Gacesa, R F Venn.   

Abstract

N6-(6-Aminohexylcarbamoylmethyl)-NAD+ was coupled to lactate dehydrogenase by using glutaraldehyde to form an active complex. The stability of this complex could be considerably improved by reduction with KBH4, although this treatment caused a partial decrease in specific activity. NAD+ was also coupled directly to the enzyme by this method. All of these complexes exhibited an intrinsic activity in the absence of exogenous NAD+.

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Year:  1979        PMID: 218564      PMCID: PMC1186378          DOI: 10.1042/bj1770369

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  5 in total

1.  Covalent binding of an NAD analogue to liver alcohol dehydrogenase resulting in an enzyme-coenzyme complex not requiring exogenous coenzyme for activity.

Authors:  M O Månsson; P O Larsson; K Mosbach
Journal:  Eur J Biochem       Date:  1978-05-16

2.  A novel method of coenzyme immobilization [proceedings].

Authors:  P Gacesa; W J Whish
Journal:  Biochem Soc Trans       Date:  1977       Impact factor: 5.407

3.  A new immobilized NAD+ analogue, its application in affinity chromatography and as a functioning coenzyme.

Authors:  M Lindberg; P O Larsson; K Mosbach
Journal:  Eur J Biochem       Date:  1973-12-03

4.  Preparation of an alcohol-dehydrogenase--NAD(H)--sepharose complex showing no requirement of soluble coenzyme for its activity.

Authors:  S Gestrelius; M O Månsson; K Mosbach
Journal:  Eur J Biochem       Date:  1975-09-15

5.  The immobilization of adenine nucleotides on polysaccharides by using glutaraldehyde coupling and borohydride reduction.

Authors:  P Gacesa; W J Whish
Journal:  Biochem J       Date:  1978-10-01       Impact factor: 3.857

  5 in total

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