Abstract
Summary Sephadex G-200 gel filtration was used to fractionate guinea pig milk proteins. Four well defined components were found. The first eluted Component I with about 56.4 p. cent of the total protein area contained most of the caseinate. Lipoprotein lipase activity was found to be associated with the caseinate in component I. Characterization of the enzyme was accomplished by means of inhibition experiments and substrate specificity. It was concluded that lipoprotein lipase activity associated with casein micelles appeared as a distinct lipase of guinea pig skim milk.
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