Purification and characterization of carnosine synthetase from mouse olfactory bulbs
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Purification, specific activity, cofactor needs and substrate specificity of carnosine synthetase from mouse olfactory bulb.
What the authors reported
The enzyme was purified about 500-fold to a specific activity near 25 nmol/min/mg, about 11 times that of the chicken pectoral muscle enzyme. ATP was required and could not be replaced by ADP. Histidine analogues such as 1- and 3-methylhistidine competitively inhibited synthesis; among beta-alanine analogues only GABA and beta-amino-n-butyric acid were incorporated.
Limits of this study
Enzyme biochemistry in mouse tissue. Abstract not available in PubMed to cross-check. Full text not read.
Source
PubMed 100576 · doi:10.1111/j.1471-4159.1978.tb00127.x
Entry checked against OpenAlex record (abstract); the PubMed record has no abstract, so this entry could not be checked against PubMed on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.