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Biomembranes pp 105-119 | Cite as

Membrane Associated Proteins

  • Sidney Fleischer
  • Warren L. Zahler
  • Hidehiro Ozawa

Abstract

One approach to the study of membrane arrangement is to try to tease away membrane components and observe the effect of such treatment on ultrastructure. We found earlier that lipid can be removed from the mitochondrial inner membranes with retention of the characteristic trilaminar appearance of this membrane (1). This observation meant that the simple Dayson-Danielli model of the membrane (2) i.e., a bilayer of phospholipid sandwiched by protein could not be correct for this membrane. If so, the protein ends should collapse or become irregular when the supporting central layer was removed. However, the trilayer was retained in the absence of lipid (1). To salvage the Dayson-Danielli model supporters of this hypothesis must at least postulate that protein cross-links are present to buttress the structure.

Keywords

Membrane Associate Protein Residue Fraction Rough Microsome Urea Extraction Beef Heart Mitochondrion 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1971

Authors and Affiliations

  • Sidney Fleischer
    • 1
  • Warren L. Zahler
    • 1
  • Hidehiro Ozawa
    • 2
  1. 1.Department of Molecular BiologyVanderbilt UniversityNashvilleUSA
  2. 2.Department of AnatomyNiigata UniversityNiigataJapan

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