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Effects of in vitro N-glucosylation on type-I collagen fibrillogenesis
- Source :
- Bioscience Reports. 1:945-954
- Publication Year :
- 1981
- Publisher :
- Portland Press Ltd., 1981.
-
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.
- 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
Subjects
Details
- ISSN :
- 15734935 and 01448463
- Volume :
- 1
- Database :
- OpenAIRE
- Journal :
- Bioscience Reports
- Accession number :
- edsair.doi.dedup.....9c501de8860670300951ebc3462303c0