Separation and characterization of two carnosine-splitting cytosolic dipeptidases from hog kidney (carnosinase and non-specific dipeptidase)
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- High-performance anion-exchange separation and kinetic characterisation of two carnosine-hydrolysing cytosolic dipeptidases from hog kidney, and carnosinase activity in hog and rat brain and liver.
What the authors reported
Both enzymes were cytosolic and were activated and stabilised by manganese and dithiothreitol. Peak I (carnosinase) had a Km of 0.4 mM carnosine, pI 5.5 and Mr 57,000, and also carried the activities earlier called homocarnosinase and manganese-independent carnosinase. Peak II had a Km of 5 mM, pI 5.0 and Mr 70,000 and was inhibited by bestatin and leucine. Hog and rat brain and liver carnosinase activity was completely inhibited by bestatin, which the author took to mean those organs contain peak II with little or no peak I. The author recommends calling peak II the non-specific cytosolic dipeptidase.
Limits of this study
Enzyme study in pig kidney. Full text not read.
Source
PubMed 2378680 · doi:10.1515/bchm3.1990.371.1.433
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.