A new method for the study of glutaraldehyde-induced crosslinking properties in proteins with special reference to the reaction with amino groups.
J Histochem Cytochem, 1978/5;26(5):412-4.
Molin SO, Nygren H, Dolonius L
PMID: 96177
Impact factor: 4.137
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.
MeSH terms
Aldehydes; Amines; Amino Acids; Chemical Phenomena; Chemistry; Glutaral; Horseradish Peroxidase; Proteins; Sepharose
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