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Mass spectrometry assay for studying kinetic properties of dipeptidases: characterization of human and yeast dipeptidases

Pandya V, Ekka MK, Dutta RK, et al.. Analytical Biochemistry, 2011; 418(1):134-142.

Laboratory studyHumansOther animals

Design
Laboratory study
What was measured
Steady-state Km and turnover rates of human carnosinases CN1 and CN2 and yeast Dug1p by an ESI-MS assay, compared with RP-HPLC, and carnosine levels in CHO cells over time by MS/MS.

What the authors reported

At pH 8.0 the turnover rates of CN1 and CN2 were 112.3 and 19.5 per second, making CN1 about 6-fold more efficient; CN2 turnover rose 4-fold at pH 9.2 with no change in Km. Results agreed with the HPLC assay, and the method also measured carnosine in CHO cells without substrate modification.

Limits of this study

Enzyme kinetics and method development. Abstract only.

Source

PubMed 21771575 · doi:10.1016/j.ab.2011.06.029

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.