The mechanochemical protein kinesin is believed to play an important role in intracellular vesicle movements, including the anterograde motion of axoplasmic transport. This article reviews some of the pharmacological and biochemical information about kinesin, particularly with respect to the properties of nucleotide-dependent microtubule binding, microtubule-activated ATPase activity, and kinesin-driven microtubule translocation. The implications of this information on the mechanochemical mechanisms of kinesin are discussed and a brief comparison of kinesin with two other mechanochemical proteins, myosin and dynein, is also given.