Ultraviolet Absorption Spectrum of Bovine Phosphatase in Presence and Absence of Added Substrate

Abstract

Summary

The ultraviolet absorption spectrum of bovine intestinal and kidney phosphatase indicates a maximum at 278 mμ, a minimum at 253 mμ and “end absorption” below 236 mμ. The absorption curve resembles that of typical proteins and suggests that phosphatase is a globulin. Tyrosin and tryptophane in the phosphatase may largely account for its characteristic absorption. No spectroscopic evidence was found for the formation of an enzyme-substrate complex when sodium β-glycerophosphate was added to a phosphatase solution.