Quantitation of human red blood cell fixation by glutaraldehyde
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.
© 1971 The Rockefeller University Press. Submitted: 9 April 1970; Revision received 10 July 1970. The authors would like to thank Mr. John Devaney and the Jet Propulsion Laboratory for their assistance in scanning microscopy, and Dr. H. J. Meiselman and Dr. S. Lang for helpful discussions and criticisms. This work was supported in part by grants HE-08977 and HE-07976 of the National Heart Institute.
Published - MORjcb71.pdf