A new method for the study of glutaraldehyde-induced crosslinking properties in proteins with special reference to the reaction with amino groups.
Open Access
- 1 May 1978
- journal article
- research article
- Published by SAGE Publications in Journal of Histochemistry & Cytochemistry
- Vol. 26 (5), 412-414
- https://doi.org/10.1177/26.5.96177
Abstract
A new method for the study of glutaraldehyde reactions with proteins is presented. Glutaraldehyde-reacted protein is in a first step isolated and then in a second step reacted with aminohexyl groups bound to Sepharose particles. This reaction is linear at low protein concentrations and proceeds rapidly when proteins are reacted with 100-fold and 1000-fold molar excess of glutaraldehyde. This method enables the study of glutaraldehyde-induced crosslinking properties of the modified proteins as an isolated property with high reliability.This publication has 6 references indexed in Scilit:
- Reaction of proteins with glutaraldehydeArchives of Biochemistry and Biophysics, 1968
- PURIFICATION AND QUANTITATION OF GLUTARALDEHYDE AND ITS EFFECT ON SEVERAL ENZYME ACTIVITIES IN SKELETAL MUSCLEJournal of Histochemistry & Cytochemistry, 1967
- Preparation of enzymically active, water-insoluble derivatives of trypsinArchives of Biochemistry and Biophysics, 1967
- The Enzymic Behavior of Carboxypeptidase-A in the Solid State*Biochemistry, 1966
- A TECHNIQUE FOR LIGHT AND ELECTRON MICROSCOPIC IDENTIFICATION OF ADRENALIN- AND NORADRENALIN-STORING CELLSJournal of Histochemistry & Cytochemistry, 1964
- INTERMOLECULAR CROSS LINKING OF A PROTEIN IN THE CRYSTALLINE STATE: CARBOXYPEPTIDASE-AProceedings of the National Academy of Sciences, 1964