Formation of protein micelles from amphiphilic membrane proteins.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 11 ·1978-11-00 ·Pages 5306-10

Simons K, Helenius A, Leonard K, Sarvas M, Gething MJ

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

Antibodies Bacillus/enzymology Colloids Glycoproteins Membrane Proteins Micelles Microscopy, Electron Molecular Weight Parainfluenza Virus 1, Human Penicillinase Semliki forest virus Viral Proteins

Chemicals

Antibodies Colloids Glycoproteins Membrane Proteins Micelles Viral Proteins Penicillinase

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Simons K

Helenius A

Leonard K

Sarvas M

Gething M J

References (27)

27 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.75.11.5306

Published

1978-11-00

Pages

5306-10

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC392951

Subset

External Links

PubMed source DOI: 10.1073/pnas.75.11.5306 PMC Full Text View journal details

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