Abstract
Adult guinea-pig dermis collagen is extensively soluble in 0.2M acetic acid whereas young dermal scar tissue collagen is not and moreover cannot be dispersed to any great extent in 0.2M acetic acid after pretreatment with EDTA or crude bacterial α-amylase.Extraction of adult guinea-pig dermis with neutral salt and EDTA yields an insoluble collagen showing little evidence of impurity on the basis of its amino acid composition and hexosamine content. The same procedures applied to dermal scar tissue yield a collagen which appears to be firmly associated with a hexose rich protein. A purer scar collagen preparation is obtained after digesting the insoluble collagen with the α-amylase.Although there are obvious differences in the fibril diameters of the two collagens, the extent of hydroxylysine glycosylation is similar in both but the proportions of mono- and disaccharide substitutions are quite distinct.
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