摘要：

The lipophilic protein moieties of human low density lipo- protein, Semliii Forest virus envelope, and human erythro- cyte stroma were obtained lipid-free with the use of sodium deoxycholate treatment and gel filtration in deoxycholate- containing media. Detergent binding was determined by subjecting the proteins to gel filtration in the presence of micellar concentrations of radioactive deoxycholate or the nonionic detergent Triton X-100. The amount of detergents bound to the proteins could be measured from the amount of radioactive detergent that co-eluted with the protein. The lipophilic proteins bound large amounts of deoxycholate and Triton X-100 (up to about 70% of their weight). The hydrophilic proteins tested bound little or no deoxycholate or Triton X-100.

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