Purification of the growth-related protein p25 of the Ehrlich ascites tumor and analysis of its isoforms.
1. Two of the three isoforms of the growth-related protein p25 of the Ehrlich ascites tumor have been purified to homogeneity by giant two-dimensional polyacrylamide gel electrophoresis. 2. Antibodies raised against the isoform p25/1 react also with isoforms p25/2 and p25/3. 3. Limited tryptic digestion of p25/1 and p25/2 resulted in similar oligopeptide patterns. Corresponding oligopeptides of both isoforms have identical amino acid sequences. 4. The isoforms p25/2 and p25/3 are phosphorylated derivatives of unphosphorylated p25/1. The phosphorus is bound to serine and a further unknown phosphorylation site.
Benndorf
R
R
Department of Cell Physiology, Central Institute of Molecular Biology, Berlin-Buch.
Kraft
R
R
Otto
A
A
Stahl
J
J
Böhm
H
H
Bielka
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000032:analysis* / Q000473:pathology; D002455:Cell Division; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins; D007120:Immunochemistry; D051379:Mice; D018832:Molecular Chaperones; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000276:immunology / Q000302:isolation & purification* / Q000502:physiology; D010446:Peptide Fragments / Q000302:isolation & purification; D010766:Phosphorylation; D014357:Trypsin
D006360:Heat-Shock Proteins; C486113:Hsbp1 protein, mouse; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D010446:Peptide Fragments; D014357:Trypsin