Hydrolysis and binding of leucine enkephalin to lymphomic and erythroleukaemic cell lines.
Hydrolysis and binding of labelled leucine enkephalin have been measured in the presence of cell lines of lymphoid and erythroid origin. The radioactive label was found to be associated to all lines studied. In the presence of these cells, enkephalin is rapidly hydrolyzed, forming three tyrosine-containing peptides: Tyr, Tyr-Gly and Tyr-Gly-Gly. Conversely, the presence of selective protease inhibitors reduces both enkephalin degradation and binding. Data obtained suggest the involvement in enkephalin hydrolysis of aminopeptidases, dypeptidylaminopeptidases and dypeptidylcarboxypeptidases. In addition, they suggest that the radioactive label associated to cells can be related to the peptides formed by the enzyme degradation of enkephalin and not to the intact pentapeptide.
Dipartimento di Medicina Sperimentale e Scienze Biochimiche, II Università degli Sudi di Roma Tor Vergata, Italy.
G
G
Roscetti
L
L
Bongiorno
A
A
Urbani
M
M
Marini
L G
LG
Roda
D000595:Amino Acid Sequence; D002855:Chromatography, Thin Layer; D004743:Enkephalin, Leucine / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D008214:Lymphocytes / Q000378:metabolism; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010447:Peptide Hydrolases / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D014407:Tumor Cells, Cultured
D011480:Protease Inhibitors; D004743:Enkephalin, Leucine; D010447:Peptide Hydrolases