Crosslinking and labeling of membrane proteins by transglutaminase-catalyzed reactions.

作者：Anne Dutton, Sherwin J. Singer · 发表于：Proceedings of the National Academy of Sciences · 年份：1975 · DOI：10.1073/pnas.72.7.2568 · 被引用次数：61 · 研究领域：Blood properties and coagulation、Erythrocyte Function and Pathophysiology、Lipid Membrane Structure and Behavior

Transglutaminase enzymes catalyze for the formation of epsilon(gamma-glutamyl)lysyl crosslinks, or the substitution of a variety of primary amines for the amide function of protein-bound glutaminyl residues. These enzymes should therefore be useful in crosslinking the proteins of membranes and in attaching a variety of chemical probes and labels to these proteins. This usefulness is demonstrated in experiments with the enzyme liver transglutaminase and the membranes with the enzyme liver transglutaminase and the membranes of mouse erythrocytes and of rabbit skeletal muscle sarcoplasmic reticulum.