Mean sizes of peptides generated and number of cuts made in a single polypeptide chain by proteasomes in rabbit muscle and Thermoplasma

Range Table - link
Organism Various
Reference Kisselev AF, Akopian TN, Woo KM, Goldberg AL. The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation. J Biol Chem. 1999 Feb 5 274(6):3363-71. p.3367 table 1PubMed ID9920878
Primary Source Kisselev AF, Akopian TN, Goldberg AL. Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J Biol Chem. 1998 Jan 23 273(4):1982-9.PubMed ID9442034
Method P.3364 left column 3rd paragraph: "In these studies, four proteins of different lengths (casein, lactalbumin, insulin-like growth factor 1 (IGF), and ovalbumin) were used as substrates after denaturation, which appears to be necessary for proteins to traverse the narrow opening in the a-rings of the 20 S proteasomes (ref 12)."
Comments P.3367 right column bottom paragraph: "Surprisingly, despite the very different number, arrangement, and specificities of their active sites, the size distribution of the products of the mammalian proteasomes (Fig. 5) had a similar shape, mean size (Table I), and size range as the peptides generated by proteasomes from archaea T. acidophilum (primary source). For example, with IGF as a substrate, the mean sizes of peptides released by rabbit 20 S proteasome were the same as those generated by its archaeal counterparts (Table I)."
Entered by Uri M
ID 109952