A new method for the study of glutaraldehyde-induced crosslinking properties in proteins with special reference to the reaction with amino groups.
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.
D000447:Aldehydes; D000588:Amines; D000596:Amino Acids; D055598:Chemical Phenomena; D002621:Chemistry; D005976:Glutaral; D006735:Horseradish Peroxidase; D011506:Proteins / Q000302:isolation & purification; D012685:Sepharose / Q000031:analogs & derivatives
D000447:Aldehydes; D000588:Amines; D000596:Amino Acids; D011506:Proteins; D012685:Sepharose; D006735:Horseradish Peroxidase; D005976:Glutaral