Polypeptides produced by hydrolysis of collagen from minced animal hide and skin scraps were studied by mass spectrometry (MS) in conjunction with electrophoresis to det. their moL mass. The degree of peptides ionisation was ca 50+. This allowed for observation of the large poly peptide chains with mass analyzers with a relatively low m/z range. The electrospray and atm. pressure photoionization techniques were used. The polypeptide fractions formed during the hydrolysis of collagen were easily identified. The moL mass of the products was 28-82 kDa.