[Fibril formation in solutions of solubilized collagen].
Influence of the preparations of bacterial proteinases, protorisine and prototerrisine, was studied on the stability of the mature collagen of beef skin. The chemical composition of the tissue has been shown to be changed by these enzymes inconsiderably. The tissue treated by orisine and terrisine is completely dissolved in 0.5 M acetic acid (solubilized collagen). When the solutions of such collagen are heated to 37 degrees within the pH range from 4 to 10 at the ionic strength of 0.25 fibrils are formed. Under electron microscope fibres are cross-striated that is typical of native collagen fibres with periodicity of about 640 A. After chilling to 4 degrees, a part of fibrils is dissolved again. Nephlometry was used to study the rate of fibril formation as a function of pH and temperature values. A conclusion has been drawn that the mature collagne dissolved after incubation with bacterial proteinases is close to the acid-soluble collagen fraction in the ability to produce fibres upon heating.
D001665:Binding Sites; D003094:Collagen; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D009994:Osmolar Concentration; D011485:Protein Binding; D011487:Protein Conformation; D012995:Solubility
D046911:Macromolecular Substances; D003094:Collagen
Fibrilloobrazovanie iz rastvorov soliubilizirovannogo kollagena