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Electron-microscopical approach to a structural model of intima collagen
The Biochemical Journal
|May 1, 1983
Summary
Researchers identified the unique structure of intima collagen, revealing its monomeric unit and how it forms dimers, tetramers, and fibrous structures. This unique collagenous protein is proposed as type VI collagen.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Collagen is a crucial structural protein in connective tissues.
- The specific structure and assembly of intima collagen were not well understood.
Purpose of the Study:
- To elucidate the molecular structure and assembly of intima collagen.
- To characterize the different oligomeric forms of intima collagen.
Main Methods:
- Electron microscopy (rotary shadowing, negative staining)
- Analytical ultracentrifugation
- Selective reduction of interchain disulphide bridges
- Bacterial collagenase digestion
Main Results:
- Identified a monomeric unit (Mr 170,000) with a triple helix and distinct globular domains.
- Characterized dimers as anti-parallel staggered aggregates and tetramers as covalently linked structures.
- Observed fibrous forms assembled from tetramers with overlapping outer segments.
- Demonstrated that only outer helical segments are degraded by collagenase.
Conclusions:
- Intima collagen exhibits a unique structure, suggesting a microfibrillar origin.
- Proposed the designation of this unique collagenous protein as type VI collagen.