Abstract
The chymotryptic digestion of cortical cells from Merino wool fibers separated clean microfibrils and liberated a small amount of keratinous protein called the dissolved protein. During the purification of microfibrils by a short sonication coupled with differential centrifugation, a tiny amount of globular protein, as examined under electron microscope, was also liberated. These two proteins are analyzed for their chemical compositions, which are discussed in light of the helical configuration and the preferential attack of α-chymotrypsin on the various amino acid residues in these two dispersed proteins.
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