Abstract
The homogeneity of wool SCMK-B2 and mohair SCMK-B2, prepared according to the procedure of Gillespie, has been investigated. Moving boundary electrophoresis and gel filtration of the preparations revealed a single peak. Examination of the SCMK-B2 preparations by disc electrophoresis demonstrated the presence of various components. The preparations were each separated by chromatography on DEAE-cellulose into four subfractions. The aminoacid composition and tryptic peptide patterns of the subfractions were similar but certain characteristic differences were obvious.
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