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Immobilized enzymes at the surface of rat heart muscle mitochondria
Abstract:
Of the three pairs of complementary replicas mentioned in the previous paper (1985, J. Ultrastruct. Res. 91, 38-50) one pair consisted of fracture faces exposing the cytoplasmic surface of the outer surface membrane while the complementary face exposed the cytosol at the membrane surface. The latter face was particulate with randomly distributed particles in the size range of 100 to 200 A. These particles could be shown to be located in the cytosol at the membrane surface. They qualify as particles that are loosely bound to this surface, and it is proposed that at least part of these particles consist of glycolytic enzymes.
Insights
This study reveals particles on the cytoplasmic surface of the outer membrane. These particles, 100-200 A in size, are likely glycolytic enzymes loosely bound to the cell surface.
Area of Science:
- Cell Biology
- Biochemistry
Background:
- Previous research identified complementary replicas of cell membranes.
- Understanding the composition of the cell surface and associated structures is crucial for cellular function.
Purpose of the Study:
- To characterize the particulate structures observed on the cytoplasmic face of the outer cell membrane.
- To investigate the potential identity and localization of these membrane-associated particles.
Main Methods:
- Utilized complementary freeze-fracture electron microscopy to expose membrane surfaces.
- Analyzed the size and distribution of particles on the cytoplasmic face of the outer membrane.
Main Results:
- Identified a particulate face on the cytoplasmic side of the outer membrane replica.
- Observed randomly distributed particles ranging from 100 to 200 Angstroms.
- Confirmed the localization of these particles to the cytosol at the membrane surface.
Conclusions:
- The observed particles are loosely bound to the cytoplasmic membrane surface.
- It is proposed that these particles represent, at least in part, glycolytic enzymes.