ausblenden:
Schlagwörter:
Amino Acid Sequence; Animal; Cattle; Chromatography, High Pressure Liquid; Cysteine Endopeptidases/ch [Chemistry]; *Cysteine Endopeptidases/me [Metabolism]; Hemoglobins/ch [Chemistry]; Hemoglobins/me [Metabolism]; Human; Insulin/ch [Chemistry]; *Insulin/me [Metabolism]; Models, Molecular; Molecular Sequence Data; Multienzyme Complexes/ch [Chemistry]; *Multienzyme Complexes/me [Metabolism]; *Thermoplasma/en [Enzymology]
Zusammenfassung:
Analysis of the degradation products from two proteins, the insulin B-chain and human hemoglobin, generated by archaebacterial Thermoplasma acidophilum 20 S proteasomes, revealed an unexpectedly broad specificity. In spite of the vast number of different peptides found, they fell into a rather narrow size range. This suggests that a molecular ruler exists which determines the length of the cleavage products.
