Purification and properties of human serum carnosinase
Laboratory studyHumansOther animals
- Design
- Laboratory study
- What was measured
- Purification of carnosinase from human plasma, its physical properties, substrate preference, tissue distribution relative to trapped blood, and presence in the serum of 6 higher primates and 12 non-primate mammals.
What the authors reported
Human serum carnosinase was purified 18,000-fold; it is a glycoprotein dimer (subunit Mr 75,000, pI 4.4) linked by disulfide bonds, most active on carnosine and anserine and preferring C-terminal histidine dipeptides. Tissue content was proportional to trapped blood except in brain, which held about 9 times more than expected, consistent with a role in hydrolysing homocarnosine. Serum carnosinase was present in six higher primates but absent in twelve non-primate mammals, except the Golden hamster, which had a distinct carnosinase.
Limits of this study
Biochemical study; the species comparison underpins the caution that rodent oral carnosine data do not transfer to people. Abstract only.
Source
PubMed 1903095 · doi:10.1016/0009-8981(91)90073-l
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.