Abstract
In order to estimate the molecular weights of proteins the analytical conditions of GPC and HPLC were investigated. Under presence of 0.2% SDS and 0.5M sodium phosphate buffer (pH 7.0), the plots of molecular weight versus retention time were linear in the range of 3000 to 150000 molecular weights. Furthermore, rough coformation of proteins were surmisable by analysis of changes in GPC chromatogram after denatured with 2-mercaptoethanol.
Retention times of small peptides on reversed-phase HPLC depend on their hydrophobisity. Molecular weights of peptides could be estimated by their retention times. This method is useful to estimate the molecular weights of small peptides and for pattern analysis of hydrolyzed peptides.
Proteins could be classified by analysis of their amino acids composition because they are characteristic for each proteins.
It is very effective for analysis of proteins in cosmetics and characterizing unknown proteins by combination of these methods.
