Published April 18, 1989
| Version v1
Journal article
Isotope effects on binding of NAD+ to lactate dehydrogenase
Description
The isotope effect on binding [4-2H]NAD+ and [4-3H]NAD+ to lactate dehydrogenase has been shown to be 1.10 +/- 0.03 by whole molecule isotope ratio mass spectrometry and 1.085 +/- 0.01 by 3H/14C scintillation counting. These values demonstrate that specific interactions of the nicotinamide ring with the enzyme make the C-H bond at C-4 less stiff in the binary complex
Additional details
Publishing Information
- Journal Title
- Biochemistry
- Journal Volume
- 28
- Journal Issue
- 8
- Series
- Biochemistry.
- Journal Page Range
- 3619-3624
- ISSN
- 0006-2960
- CODEN
- BICHA
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 21006104
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- BIOCHEMICAL REACTION KINETICS; CARBON 14 COMPOUNDS; DEUTERIUM; IN VITRO; ISOTOPE EFFECTS; ISOTOPE RATIO; LACTATE DEHYDROGENASE; MASS SPECTROSCOPY; MOLECULAR STRUCTURE; NAD; NICOTINAMIDE; RECEPTORS; SCINTILLATION COUNTING; TRITIUM COMPOUNDS
- Descriptors DEC
- AMIDES; AZINES; CARBON COMPOUNDS; COENZYMES; COUNTING TECHNIQUES; DEHYDROGENASES; ENZYMES; HETEROCYCLIC COMPOUNDS; HYDROGEN COMPOUNDS; HYDROGEN ISOTOPES; ISOTOPES; KINETICS; LIGHT NUCLEI; NUCLEI; NUCLEOTIDES; ODD-ODD NUCLEI; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; OXIDOREDUCTASES; PYRIDINES; REACTION KINETICS; SPECTROSCOPY; STABLE ISOTOPES; VITAMIN B GROUP; VITAMINS