During his years working as a physician Michaelis and a friend (Peter Rona) built a compact lab, in the hospital, and over the course of five years – Michaelis successfully became published over 100 times. During his research in the hospital, he was the first to view the different types of inhibition; specifically using fructose and glucose as inhibitors of maltase activity. Maltase breaks maltose into two units of either glucose or fructose. Findings from that experiment allowed for the divergence of non-competitive and competitive inhibition. Non-competitive inhibition effects the "kcat" value (but not the Km) on any given graph; this inhibitor binds to a site that has specificity for the certain molecule. Michaelis determined that when the inhibitor is bound, the enzyme would become inactivated.