Electron microscope studies of deaminated and crosslinked collagen
- 2 August 1970
- journal article
- Published by Wiley in Journal of Microscopy
- Vol. 92 (1) , 27-30
- https://doi.org/10.1111/j.1365-2818.1970.tb02233.x
Abstract
SUMMARY: Glutaraldehyde‐crosslinked rat‐tail collagen, compared with native fibres, showed an increase in the size of the light bands when examined in the electron microscope using a negative‐staining technique. Collagen deaminated with nitrous acid gave similar patterns to native fibres and showed no change after treatment with glutaraldehyde. It was concluded that the increase in the size of the light bands is due to the formation of intermolecular crosslinks rather than charge neutralization of lysine amino groups.Keywords
This publication has 4 references indexed in Scilit:
- The structure and assembly of collagen fibrils*: II. An electron-microscope study of cross-linked collagenJournal of the Royal Microscopical Society, 1967
- The structure and assembly of collagen fibrils*: I. Native‐collagen fibrils and their formation from tropocollagenJournal of the Royal Microscopical Society, 1967
- New Model for the Tropocollagen Macromolecule and its Mode of AggregationNature, 1965
- Electron microscope studies on the structure of collagen fibrils by negative stainingCell and tissue research, 1962