Abstract
The reaction of polylysine and 1-butanal afforded 2-ethyl-2-hexenal, an aldol condensation and dehydration product of 1-butanal. 1-Butanal and 2-ethyl-2-hexenal were able to form fluorescence in polylysine, bovine serum albumin and erythrocyte membrane proteins. They were able to cross-link polylysine, hemoglobin, erythrocyte membrane proteins and isolated spectrin. Formation of cross-links by these aldehydes depended of the kind of protein. The ability of the proteins to form cross-links may reflect the contents of functional groups respomsible and the quaternary structures of the proteins. 1-Butanal and 2-ethyl-2-hexenal may participate in the formation of cross-links and fluorescence by interaction with amino groups in the proteins.
