Abstract
Summary
The effects of certain enzymic and other treatments of β-lipovitellin of egg yolk were studied in a medium of 1 M sodium chloride-0.037 M potassium phosphate (pH 6.8), which allowed predominant distribution of dimer form in native β-lipovitellin. Ultracentrifugal analysis of β-lipovitellin incubated with the surface-active agents, Triton X-100 and Tween 20, and with snake venom phospholipase A resulted in an increase in the percentage of slow-sedimenting component corresponding to monomer β-lipovitellin. Although treatment of β-lipovitellin with α-chymotrypsin also caused a sizable decrease in the proportion of associated lipovitellin, a similar treatment of β-lipovitellin with trypsin caused no appreciable change in the relative amounts of monomer and dimer components. Exposure to papain resulted in a series of overall changes in Schlieren sedimentation pattern of the lipoprotein with incubation time.
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