Myosin Myosin Myosins () are a superfamily of motor proteins best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes. They are ATP-dependent and responsible for actin-based motility. The term was originally used to describe a group of similar ATPases found in the cells of both striated muscle tissue and smooth muscle tissue. Following the discovery by Pollard and Korn (1973) of enzymes with myosin-like function in "Acanthamoeba castellanii", a global range of divergent myosin genes have been discovered throughout the realm of eukaryotes. Although myosin was originally thought to be restricted
Lectin their particular high specificity for foreign glycoconjugates (e.g. those of fungi, invertebrates, and animals) and used in biomedicine for blood cell testing and in biochemistry for fractionation. Although they were first discovered more than 100 years ago in plants, now lectins are known to be present throughout nature. It is generally believed that the earliest description of a lectin was given by Peter Hermann Stillmark in his doctoral thesis presented in 1888 to the University of Dorpat. Stillmark isolated ricin, an extremely toxic hemagglutinin, from seeds of the castor plant ("Ricinus communis"). The first lectin to be purified on a