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Lipoprotein lipase is heterogeneous, and it was suggested that the enzyme in adipose tissue is transformed from a species of mol. wt. approx. 120000 to forms of much higher molecular weight as it is secreted from the fat-cell. This paper demonstrates that the forms of higher molecular weight are probably artifacts. Enzyme preparations were characterized by gel filtration, by density-gradient centrifugation and by affinity chromatography. The results indicate that the enzyme forms of mol. wt. greater than 120000 result from an association of the enzyme with particulate material. It is therefore necessary to reconsider schemes that have recently been proposed for the synthesis and export of lipoprotein lipase.

The heterogeneity of the lipoprotein lipase of rat epididymal adipose tissue