Purification and partial characterization of two acid phosphatase forms from pearl oyster (Pinctada fucata)

Academic Article

Abstract

  • The present study describes the details about the acid phosphatase forms in the pearl oyster, Pinctada fucata. Two isoenzymes (AcPase I and II) of acid phosphatase were separated and purified from viscera of pearl oyster, P. fucata to homogeneity by chromatography on DEAE-Sepharose Fast Flow, Sephadex G-200 superfine and ConA Sepharose 4B, and partial biochemical properties of AcPase I and II were studied. AcPase I and AcPase II had molecular weights of 208.8 and 64.3 kDa, respectively. AcPase I was a single polypeptide chain, while AcPase II was a dimeric enzyme composed of two equivalent subunits. AcPase I and II showed optimal pHs at 4.6 and 3.2 with p-nitrophenylphosphate as substrate. The optimal catalytic reaction temperature was 47°C for AcPase I and 57°C for AcPase II. Both enzyme forms were stable when incubated at 50°C for 40 min. Tartrate and fluoride were the most effective inhibitors of the enzymes. Fe3+, Zn2+, Cu2+ and Pb2+ inhibited the activity of AcPase I and II to differing extents. AcPase I and II were apparently nonspecific and hydrolyzed various phosphoric esters. The different properties of AcPase I and II suggested that the two enzymes may play different roles in the pearl oyster. © 2005 Elsevier Inc. All rights reserved.
  • Authors

    Digital Object Identifier (doi)

    Author List

  • Jing G; Li L; Li Y; Xie L; Zhang R
  • Start Page

  • 229
  • End Page

  • 235
  • Volume

  • 143
  • Issue

  • 2