Phosphoglycollate Phosphatase in Marine Algae: Isolation and Characterization from Halimeda cylindracea

Abstract

Phosphoglycollate phosphatase was partially purified (107-fold) from the marine alga H. cylindracea. The partially purified enzyme was almost completely specific for phosphoglycollate as substrate, and had the following properties: a specific activity of 2.73, an apparent K_m for phosphoglycollate of 8 x 10^-4M, a pH optimum of 7.5 - 8 and a divalent cation requirement. The presence of the enzyme is discussed in relation to photorespiration in this alga.