1. Effects of in vitro N-glucosylation on type-I collagen fibrillogenesis
- Author
-
A. Le Pape, J.D. Guitton, P. Y. Sizaret, and J.P. Muh
- Subjects
Time Factors ,Chemistry ,Temperature ,Biophysics ,Fibrillogenesis ,macromolecular substances ,Cell Biology ,Fibril ,Biochemistry ,In vitro ,Rats ,law.invention ,Hydrophobic effect ,Microscopy, Electron ,Collagen, type I, alpha 1 ,Glucose ,Nephelometry and Turbidimetry ,law ,Animals ,Collagen ,Turbidimetry ,Electron microscope ,Molecular Biology ,Type I collagen - Abstract
Acid-soluble collagen from rat tail tendon was glucosylated in vitro and fibrillogenesis parameters were determined first at 35 degrees C then at 4 degrees C. Increased lag phase and half time were shown to be related to the amount of non-enzymatically bound glucose, probably due to a decrease of hydrophobic interactions at this early stage of fibril formation. The absence of intermolecular cross-links and the partial redissolution of fibrils of 4 degrees C, as investigated both by turbidimetry and electron microscopy, suggests a defect in the maturation process in glucosylated collagen fibrils.
- Published
- 1981