Assembly of type I collagen fibrils de novo. Between 37 and 41 degrees C the process is limited by micro-unfolding of monomers.

摘要: The effects of temperature on the assembly collagen fibrils were examined in a system which monomers are generated de novo and physiological buffer by specific enzymic cleavage type I pC-collagen, an intermediate normal processing procollagen to collagen. Increasing reaction range 29-35 degrees C decreased turbidity lag increased rate propagation as assayed turbidity. effect gave linear Arrhenius plot with negative slope. predicted value activation energy was 113 kJ/mol. However, above 37 opposite seen at temperatures below C. In 37-41 C, markedly temperature. Also, increased. Therefore, much longer times required for reach equilibrium fibrils. A large fraction remaining solution sensitive rapid digestion trypsin alpha-chymotrypsin. Cooling solutions 25 made resistant protease digestion. results consistent conclusion that, although formation is classical example entropy-driven process self-assembly, between 41 limited reversible micro-unfolding monomer.