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PMID: 4200727 Published · ppublish English Journal Article

Relation of detergent HLB number to solubilization and stabilization of D-alanine carboxypeptidase from Bacillus subtilis membranes.

Umbreit JN, Strominger JL

Abstract

The ability of various nonionic detergents to solubilize D-alanine carboxypeptidase and other membrane-bound enzymes was correlated to a physical property of the detergent, the HLB number. Only a fairly narrow range of detergents were effective solubilizing agents. Purified carboxypeptidase required either a detergent or detergent plus a lipid fraction for stability. Only those detergents effective in solubilizing the enzyme were effective in stabilizing it.

MeSH Terms
Alanine Bacillus subtilis/cytology,enzymology Carboxypeptidases Cell Membrane/enzymology Detergents Lipids Solubility Solvents Surface-Active Agents
Chemicals
Detergents Lipids Solvents Surface-Active Agents Carboxypeptidases Alanine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Umbreit J N
Strominger J L
References (3)
3 references, click to expand
  1. Structure and synthesis of a lipid-containing bacteriophage. II. Alterations in cytoplasmic and membrane-bound enzymes during replication of bacteriophage PM2.
    Virology. 1969 Nov;39(3):408-18 PMID: 4243130
  2. Complex lipid requirements for detergent-solubilized phosphoacetylmuramyl-pentapeptide translocase from Micrococcus luteus.
    Proc Natl Acad Sci U S A. 1972 Jul;69(7):1972-4 PMID: 4340168
  3. A rapid method of total lipid extraction and purification.
    Can J Biochem Physiol. 1959 Aug;37(8):911-7 PMID: 13671378
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
Published
1973-10-00
Pages
2997-3001
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC427155
Subset
IM
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