The similarity between the primary structures of two non-histone chromosomal proteins.
A comparison has been made of two non-histone chromosomal proteins, high-mobility-group proteins 1 and 2. Peptides produced from the two proteins by various chemical and enzymic cleavages have been compared by polyacrylamide gel electrophoresis and peptide mapping. In addition the cysteine content, C-terminal sequences and amide content have been determined for both proteins. The results obtained, together with previous results, show that high-mobility-group proteins 1 and 2 have closely related primary structures, although obviously being different molecules. When analysed by isoelectric focusing both proteins exhibit complex banding patterns. In the case of high-mobility-group protein 1, this could be caused by aggregation, but with high-mobility-group protein 2 there are four distinctive subfractions focusing between pH 7.8 and 8.9.
D000577:Amides / Q000032:analysis; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002268:Carboxypeptidases; D002875:Chromosomes / Q000032:analysis; D003488:Cyanogen Bromide; D007525:Isoelectric Focusing; D009698:Nucleoproteins; D010434:Pepsin A; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D013438:Sulfhydryl Compounds / Q000032:analysis; D014357:Trypsin
D000577:Amides; D000596:Amino Acids; D009698:Nucleoproteins; D010446:Peptide Fragments; D013438:Sulfhydryl Compounds; D002268:Carboxypeptidases; D014357:Trypsin; D010434:Pepsin A; D003488:Cyanogen Bromide