QUANTITATION OF HUMAN RED BLOOD CELL FIXATION BY GLUTARALDEHYDE
Open Access
- 1 January 1971
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 48 (1), 91-100
- https://doi.org/10.1083/jcb.48.1.91
Abstract
The uptake of glutaraldehyde by human red blood cells has been measured as a function of time by a freezing point osmometer. The rate of attachment of glutaraldehyde to the cell proteins is high over the first hour, declining to zero over a period of a few days. The number of glutaraldehyde molecules cross-linking with each hemoglobin molecule is of the order of 200, in reasonable agreement with the calculated number of attachment sites. The cell membrane is immediately highly permeable to glutaraldehyde. Selective permeability to ions is lost during fixation. Ionic equilibrium is obtained only after a few hours. An optimum fixation technique for shape preservation is suggested.Keywords
This publication has 8 references indexed in Scilit:
- The impurities in commercial glutaraldehyde and their effect on the fixation of brainJournal of Ultrastructure Research, 1970
- Reaction of proteins with glutaraldehydeArchives of Biochemistry and Biophysics, 1968
- Centrifugal Packing of Suspensions of Erythrocytes Hardened with AcetaldehydeExperimental Biology and Medicine, 1968
- THE STRUCTURE OF CARBOXYPEPTIDASE A, VI. SOME RESULTS AT 2.0-Å RESOLUTION, AND THE COMPLEX WITH GLYCYL-TYROSINE AT 2.8-Å RESOLUTIONProceedings of the National Academy of Sciences, 1967
- PURIFICATION AND QUANTITATION OF GLUTARALDEHYDE AND ITS EFFECT ON SEVERAL ENZYME ACTIVITIES IN SKELETAL MUSCLEJournal of Histochemistry & Cytochemistry, 1967
- The Purity and the Osmolarity of Commercial GlutaraldehydeJournal of Electron Microscopy, 1967
- INTERMOLECULAR CROSS LINKING OF A PROTEIN IN THE CRYSTALLINE STATE: CARBOXYPEPTIDASE-AProceedings of the National Academy of Sciences, 1964
- CYTOCHEMISTRY AND ELECTRON MICROSCOPYThe Journal of cell biology, 1963