[Study of bone tissue insoluble collagen hydrolysis by Streptomyces griseus protease using the method of N-terminal analysis].

Str. griseus protease hydrolyzes essentially insoluble collagen of bone tissue, with 34.5% of protein solubilized and 6.0% of peptide bonds splitted. 60.0 M of N-terminal amino acids is formed per 10(5) g of protein, out of them 16.8 in the fraction of free amino acids, 32.3 M in the fraction of soluble DNP-peptides and 10.9 M in that of insoluble DNP-peptides. Under the effect of trypsin the amount of collagen changing to the soluble form is thrice as low and the splitted peptide bonds are ten times as low as in case of the Str. griseus protease action. The peptide bonds incorporating the N-end of serine, threonine, glycine are more available for protease. It is supposed that under used conditions Str. griseus protease hydrolyzes not only telepeptides but also the main molecule of collagen.