Abstract
The interaction of bovine pancreatic alpha-chymotrypsin with dimyristoyl phosphatidylcholine (PC) vesicles was measured turbimetrically. The protein interacted with the vesicles at NaCl concentrations of above 0.8 M. The turbidity reached a plateau on increase in the amount of either the protein or the vesicles in the presence of a fixed amount of the other component. The precipitates formed contained both PC and protein in ratios varying with the initial amount of each component. On mixing chymotrypsin and PC vesicles, time-dependent turbidity increase was high at below pH 2.5, but relatively small at neutral and alkaline pH values. Apolar interaction between the two components was confirmed by demonstrating an increase in fluorescence intensity of chymotrypsin in the presence of the PC in 1 M NaCl. The turbidity of a mixture of PC vesicles and bovine serum albumin (BSA) increased even in the absence of 1 M NaCl, whereas the turbidities of mixtures of the vesicles and lysozyme or alpha-lactalbumin did not change with time in the presence of 1 M NaCl at pH 8.0.
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