[Reduced susceptibility of nonenzymatically glucosylated peptides against proteolytic cleavage (author's transl)].
Two peptides, alpha-endorphin and beta-melanocyte stimulating hormone, were nonenzymatically glucosylated, degraded by several proteolytic enzymes and the susceptibility against proteolytic enzymes compared to the peptides in the native, nonglucosylated state. Glucosylation was controlled by thin layer chromatography revealing Rf differences between the native and glucosylated peptides. Quantitative estimation of peptides was performed applying high performance liquid chromatography. The results showed reduced susceptibility of nonenzymatically glucosylated peptides to the proteolytic enzymes (papain, chymotrypsin, trypsin and papain) applied.
D002855:Chromatography, Thin Layer; D002918:Chymotrypsin / Q000494:pharmacology; D004723:Endorphins / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism*; D009074:Melanocyte-Stimulating Hormones / Q000378:metabolism*; D010206:Papain / Q000494:pharmacology; D010434:Pepsin A / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000494:pharmacology*; D010455:Peptides / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology; D018822:alpha-Endorphin
D004723:Endorphins; D010455:Peptides; D018822:alpha-Endorphin; D009074:Melanocyte-Stimulating Hormones; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D014357:Trypsin; D010206:Papain; D010434:Pepsin A; D005947:Glucose
Verminderte Empfindlichkeit von nichtenzymatisch glukosylierten Peptiden gegenüber proteolytischem Abbau.