Type I collagen in skin of rats who were given redundant amounts of leucin, valine, methionine or phenyl alanine differed essentially from the normal level in the amino acidic composition. Considerable shifts in the value of pI of the proteins under study as compared with the normal level are found during isofocusing. When studying subunits of collagen preparations by the reverse-phase chromatography certain differences typical of each studied state are revealed in the elution profiles in normalcy and under amino acid loadings.
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