title: Properties and function of phosphatases from vascular smooth muscle.
abstract: Myosin light chain phosphatase (MLCP) activity was present in extracts from a wide variety of mammalian tissues. A partially purified preparation of bovine aortic MLCP also showed activity against phosphorylase a and p-nitrophenyl phosphate (PNP). Whether these three activities are ascribable to a single multifunctional phosphatase or to three distinct phosphatases is unknown. The three phosphatase activities coelute during gel filtration both before and after treatment with ethanol showing exclusion volumes corresponding to 240,000 and 35,000 daltons, respectively. This indicates that the enzyme is dissociable into a smaller catalytic subunit. The widespread occurrence of MLCP activity and the close parallel among MLCP, phosphorylase a phosphatase, and PNP phosphatase activities suggest that the enzyme (or enzymes) may participate in physiological processes in addition to dephosphorylation of phosphorylated myosin light chains.
mesh_terms: D000818:Animals; D001011:Aorta / Q000201:enzymology; D002118:Calcium / Q000502:physiology; D008970:Molecular Weight; D009124:Muscle Proteins / Q000378:metabolism; D009131:Muscle, Smooth, Vascular / Q000201:enzymology / Q000502:physiology*; D009218:Myosins / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D009124:Muscle Proteins; D010749:Phosphoprotein Phosphatases; D009218:Myosins; D002118:Calcium