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Iron-containing acid phosphatases: Interaction of phosphate with the enzyme from pig allantoic fluid

Journal Article


Abstract


  • Phosphate binds to the reduced, catalytically active form of pig allantoic fluid acid phosphatase (λmax = 510 nm) at pH 4.9, causing a very rapid spectral shift to a λmax of 540 nm. This spectral shift has permitted the determination of a Kd value of ∼6mM for phosphate binding to the reduced enzyme. Phosphate also greatly potentiates the conversion of the reduced form of the enzyme to a violet, catalytically inactive form. [32P] Phosphate was used to show that phosphate is bound very tightly in this violet form of the enzyme, in a 1:1 complex. The tightly bound phosphate may be removed by reduction of the enzyme or by treatment with 6 M guanidinium chloride. Some previous studies on iron-containing acid phosphatases may well have been complicated by the presence of variable amounts of tightly bound phosphate. © 1982 Academic Press, Inc.

Publication Date


  • 1982

Citation


  • Keough, D. T., Beck, J. L., de Jersey, J., & Zerner, B. (1982). Iron-containing acid phosphatases: Interaction of phosphate with the enzyme from pig allantoic fluid. Biochemical and Biophysical Research Communications, 108(4), 1643-1648. doi:10.1016/S0006-291X(82)80098-3

Scopus Eid


  • 2-s2.0-0020493437

Start Page


  • 1643

End Page


  • 1648

Volume


  • 108

Issue


  • 4

Abstract


  • Phosphate binds to the reduced, catalytically active form of pig allantoic fluid acid phosphatase (λmax = 510 nm) at pH 4.9, causing a very rapid spectral shift to a λmax of 540 nm. This spectral shift has permitted the determination of a Kd value of ∼6mM for phosphate binding to the reduced enzyme. Phosphate also greatly potentiates the conversion of the reduced form of the enzyme to a violet, catalytically inactive form. [32P] Phosphate was used to show that phosphate is bound very tightly in this violet form of the enzyme, in a 1:1 complex. The tightly bound phosphate may be removed by reduction of the enzyme or by treatment with 6 M guanidinium chloride. Some previous studies on iron-containing acid phosphatases may well have been complicated by the presence of variable amounts of tightly bound phosphate. © 1982 Academic Press, Inc.

Publication Date


  • 1982

Citation


  • Keough, D. T., Beck, J. L., de Jersey, J., & Zerner, B. (1982). Iron-containing acid phosphatases: Interaction of phosphate with the enzyme from pig allantoic fluid. Biochemical and Biophysical Research Communications, 108(4), 1643-1648. doi:10.1016/S0006-291X(82)80098-3

Scopus Eid


  • 2-s2.0-0020493437

Start Page


  • 1643

End Page


  • 1648

Volume


  • 108

Issue


  • 4