title: Formation of protein micelles from amphiphilic membrane proteins.
abstract: The membrane penicillinase (penicillin amido-beta-lactamhydrolase, EC 3.5.2.6) from Bacillus licheniformis, the Semliki Forest virus spike proteins, and the Sendai virus glycoproteins have each been isolated as soluble protein aggregates that are virtually free of lipid and detergent. The sedimentation coefficients of the complexes were 18 S, 29 S, and 43 S, respectively. Mixed aggregates containing both the virus glycoproteins and the penicillinase could also be formed. Such protein micelles may serve a number of useful purposes in membrane research.
mesh_terms: D000906:Antibodies; D001407:Bacillus / Q000201:enzymology; D003102:Colloids; D006023:Glycoproteins; D008565:Membrane Proteins; D008823:Micelles; D008854:Microscopy, Electron; D008970:Molecular Weight; D010222:Parainfluenza Virus 1, Human; D010405:Penicillinase; D012672:Semliki forest virus; D014764:Viral Proteins
chemical_list: D000906:Antibodies; D003102:Colloids; D006023:Glycoproteins; D008565:Membrane Proteins; D008823:Micelles; D014764:Viral Proteins; D010405:Penicillinase