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Electron-microscopical studies of conformational changes in dentinal phosphophoryn
Collagen and Related Research
|November 1, 1983
Summary
Researchers purified p67tinal phosphophoryn from calf molars. Structural analysis revealed that calcium ions induce more ordered protein structures, forming disc-like aggregates potentially involved in dentin mineralization.
Area of Science:
- Biochemistry
- Structural Biology
- Biomineralization
Background:
- p67tinal phosphophoryn is a protein found in developing teeth.
- Its precise structure and function in dentin mineralization are not fully understood.
Purpose of the Study:
- To isolate and purify p67tinal phosphophoryn from unerupted calf molars.
- To analyze the protein's structure in solution and in the presence of calcium ions or methanol.
Main Methods:
- Protein isolation and purification using established biochemical methods.
- Structural analysis via circular dichroism (CD) spectroscopy.
- Morphological characterization using low-angle rotary shadowing electron microscopy (EM).
Main Results:
- In aqueous solutions, p67tinal phosphophoryn formed extended, bead-like chains with variable morphology.
- Addition of calcium ions or methanol induced CD spectra indicating increased structural order.
- Electron microscopy revealed the formation of 25-30 nm disc-like aggregates upon ion/solvent addition.
Conclusions:
- The structural changes observed are consistent with the proposed role of p67tinal phosphophoryn.
- These proteins may function as calcium hydroxyapatite nucleating sites during dentin mineralization.