Glucagon- and insulin degradation by hemolysate of human erythrocytes.
Hemolysates of human erythrocytes contain a highly specific insulin- and glucagon-degrading activity which is comparable to the so-called insulin- and glucagon-degrading proteinase (IGP, EC 3.4.23.5) found in other tissues. Glucagon degradation is inhibited by its cleavage products. Insulin, proinsulin and also cleavage products of insulin are effective inhibitors of glucagon degradation. The isolated insulin A- and B-chains are also capable of inhibiting the splitting of glucagon, but a higher concentrations. On the other hand, glucagon influences insulin degradation. Naturally occurring substances within commercially available human serum albumin have remarkable inhibitory effects on the glucagon degradation.
Hildebrandt
W
W
Institute of Biochemistry, Martin-Luther University Halle-Wittenberg, GDR.
Kohnert
K D
KD
Blech
W
W
D002402:Cathepsin D / Q000037:antagonists & inhibitors / Q000097:blood*; D004912:Erythrocytes / Q000201:enzymology*; D005246:Feedback; D005934:Glucagon / Q000097:blood*; D006461:Hemolysis; D006801:Humans; D007328:Insulin / Q000378:metabolism*; D007700:Kinetics; D011384:Proinsulin / Q000494:pharmacology
D007328:Insulin; D005934:Glucagon; D011384:Proinsulin; D002402:Cathepsin D