English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The first description of a saturable iminodipeptide transport system present in human erythrocytes is given. The 1H-n.m.r. spectra of glycyl-L-proline and those of free glycine and L-proline are significantly different. This enabled the non-invasive monitoring by 1H-n.m.r. spectroscopy of the hydrolysis of the dipeptide in human erythrocytes and their lysates. The concentration-dependence of the rate of glycyl-L-proline hydrolysis by haemolysates was described by the Michaelis-Menten expression with Km = 14.1 +/- 2.4 mmol/litre and Vmax. = 130 +/- 10 mmol/h per litre of cell water. At concentrations of the dipeptide that saturated prolidase, hydrolysis of glycyl-L-proline by whole cells was approximately 130 times slower than by lysates. This rate difference indicated that transport is the rate-determining step in peptide hydrolysis by whole cells, and thus the concentration-dependence of the transport rate was determined. The membrane transport system was found to be saturable and could be described by the Michaelis-Menten expression with Kt = 4.7 +/- 0.4 mmol/litre and Vmax. = 0.997 +/- 0.026 mmol/h per litre of cell water. Numerical integration of a consistent set of differential rate equations that described a minimal model of the coupled transport-hydrolysis system successfully described prolonged time courses of peptide hydrolysis by whole cells. The simulations showed very low steady-state levels of dipeptide in the erythrocyte and very small lag periods (less than 5 min) in the progress curve describing the appearance of free amino acid inside the cells. The rates of transport of glycyl-L-proline into erythrocytes and kidney proximal-tubular epithelium were compared and the possible importance of erythrocyte prolidase in whole-body prolyl-peptide turnover is discussed.

A proton n.m.r. study of iminodipeptide transport and hydrolysis in the human erythrocyte. Possible physiological roles for the coupled system