Intermolecular interaction studies on native and enzyme-treated acid-soluble collagen.

Abstract

The aggregative properties of acid-soluble collagen, native or enzyme treated, have been studied by electric birefringence and low shear rate viscosity. A unique type of aggregate has been found, about 700 nm long for native collagen and 530 nm for pepsin treated, regardless of the acetic acid concentration in the range 1--100 mM. The number of aggregates increases with collagen concentrations, as could be expected for electrostatic interactions. On the contrary, pepsin-extracted cartilage collagen forms aggregates of covalent nature, the number of which is independent of concentration. Viscosity measurements show two different interaction mechanisms: a short distance one which can be identified with the electric birefringence-detected aggregation, and a long distance superstructure which disappears when salt is added to the solution.

• Authors: J C Bernengo, D Herbage, C Marion, B Roux
• Journal: Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 532 Issue 2 Pg. 305-14 (Feb 15 1978) ISSN: 0006-3002 [Print] Netherlands
• PMID: 341988 (Publication Type: Journal Article)

Chemical References

• Acetates
• Sodium Chloride
• Collagen
• Pepsin A
• Pronase

Topics

• Acetates
• Animals
• Birefringence
• Cartilage, Articular (metabolism)
• Cattle
• Collagen
• Electrochemistry
• In Vitro Techniques
• Pepsin A
• Pronase (pharmacology)
• Protein Denaturation
• Skin (metabolism)
• Sodium Chloride (pharmacology)
• Solubility
• Viscosity