Proton NMR spectroscopic studies of dipeptidase in human erythrocytes.
In studies on human erythrocyte metabolism in situ, high resolution (400 MHz) 1H spin-echo NMR spectroscopy was used to follow the time dependence of hydrolysis of glycylglycine and L-cysteinylglycine in intact cells and their lysates. The concentration dependence of the hydrolysis of L-cysteinylglycine was described by a rectangular hyperbola with Km, 3.5 +/- 0.6 mmol/l lysate and Vmax, 64.2 +/- 3.2 mmol/l lysate/h. We demonstrated that glycylglycine readily enters the erythrocyte and we introduce a means of analysing the data from the coupled reaction sequence; the sequence consists of transport followed by enzyme catalysed hydrolysis.
D004150:Dipeptidases / Q000097:blood*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D004150:Dipeptidases