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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.
W Hildebrandt, and
K D Kohnert, and
W Blech
January 1985,
Biomedica biochimica acta,
W Hildebrandt, and
K D Kohnert, and
W Blech
January 1982,
Journal of endocrinological investigation,
W Hildebrandt, and
K D Kohnert, and
W Blech
August 1981,
Bollettino della Societa italiana di biologia sperimentale,
W Hildebrandt, and
K D Kohnert, and
W Blech
January 1984,
Doklady Akademii nauk SSSR,
W Hildebrandt, and
K D Kohnert, and
W Blech
January 1989,
Biomedica biochimica acta,
W Hildebrandt, and
K D Kohnert, and
W Blech
November 1981,
Endocrinology,
W Hildebrandt, and
K D Kohnert, and
W Blech
January 1991,
Biochemistry international,
W Hildebrandt, and
K D Kohnert, and
W Blech
June 1974,
Diabetes,
W Hildebrandt, and
K D Kohnert, and
W Blech
January 1967,
Acta vitaminologica et enzymologica,
W Hildebrandt, and
K D Kohnert, and
W Blech
February 1975,
Biochimica et biophysica acta,
