| 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 |