Mutation of the Active Site Glutamic Acid of Human Gelatinase A: Effects on Latency, Catalysis, and the Binding of Tissue Inhibitor of Metalloproteinases-1

Human gelatinase A, a member of the matrix metalloproteinase family, is secreted from cells as the M(r) 72,000 latent precursor, progelatinase A. The autolytic removal of an N-terminal propeptide generates the M(r) 66,000 active form. Mutants of recombinant progelatinase A, altered such that the pro...

Ausführliche Beschreibung