Metabolism of glycine- and hydroxyproline-containing peptides by the isolated perfused rat kidney
- 15 July 1985
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 229 (2) , 545-549
- https://doi.org/10.1042/bj2290545
Abstract
Isolated perfused rat kidneys removed considerable quantities of glycyltyrosine, glycylhydroxyproline, tetraglycine and prolylhydroxyproline from the perfusate. The component amino acids are released into the perfusate and, in the case of the glycine-containing peptides, there is increased synthesis of serine. Removal of peptides was more than could be accounted for on the basis of filtration, so antiluminal metabolism is indicated. Metabolism of such peptides by the kidney may contribute to renal serine synthesis in vivo.This publication has 25 references indexed in Scilit:
- Peptide transport in rabbit kidney. Studies with l-carnosineBiochimica et Biophysica Acta (BBA) - Biomembranes, 1982
- The conversion of alanine into glutamine in guinea-pig renal cortex. Essential role of pyruvate carboxylaseBiochemical Journal, 1981
- Renal metabolism of amino acids and ammonia in subjects with normal renal function and in patients with chronic renal insufficiency.Journal of Clinical Investigation, 1980
- Renal filtration, transport, and metabolism of low-molecular-weight proteins: A reviewKidney International, 1979
- Renal tubular transport and catabolism of proteins and peptidesKidney International, 1979
- Effect of Nephrectomy and Enterectomy on Plasma Clearance of Intravenously Administered Dipeptides in RatsClinical Science, 1977
- A prolidase deficiency in man with iminopeptiduriaMetabolism, 1974
- Metabolism of Proinsulin, Insulin, and C-Peptide in the RatJournal of Clinical Investigation, 1973
- SERUM ALBUMIN UPTAKE IN ISOLATED PERFUSED RENAL TUBULESThe Journal of cell biology, 1972
- Regulation of Rat Liver Glutamine Synthetase: Activation by α-Ketoglutarate and Inhibition by Glycine, Alanine, and Carbamyl PhosphateProceedings of the National Academy of Sciences, 1971