Journal article
Effect of saturated phosphatidylcholines on the functional properties of reconstituted cytochrome oxidase
Biochemistry and cell biology, v 64(2)
01 Feb 1986
PMID: 3013244
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Abstract
Cytochrome oxidase was incorporated into liposomes, at various protein/lipid ratios, composed of either a phosphatidylcholine of varying chain length and symmetry or asolectin. Catalytic activity and respiratory control were assayed at two temperatures. All preparations showed higher activity at low protein/lipid ratios, but only asolectin showed respiratory control. A spectroscopic determination of the vectorial orientation of oxidase molecules showed that, for proteoliposomes with saturated lipids, 100% of oxidase molecules could be reduced by external substrate as compared with 75% for asolectin proteoliposomes. Freeze-fracture electron microscopy confirmed that oxidase was incorporated into these proteoliposomes and differential scanning calorimetry indicated that the protein induces significant disruption in the long range packing of the saturated phospholipids. We propose that the oxidase molecules in proteoliposomes formed from saturated phosphatidylcholines do not display respiratory control because they are unable to assume the transmembrane orientation necessary for full vectorial activity.
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Details
- Title
- Effect of saturated phosphatidylcholines on the functional properties of reconstituted cytochrome oxidase
- Creators
- Michael A. SingerMaria DindaMarlene YoungLeonard Finegold
- Publication Details
- Biochemistry and cell biology, v 64(2)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1986A474200003
- Scopus ID
- 2-s2.0-0022555566
- Other Identifier
- 991019184076204721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Cell Biology