Catfish liver acid phosphatases: differently glycosylated enzyme molecules with altered kinetic properties

Two forms of catfish liver acid phosphatase (AcPase I and II) were separated and purified to homogeneity and their carbohydrate compositions and some biochemical properties were studied. Evidence is given that AcPase I and II are differently glycosylated forms of the same enzyme. The enzyme forms differ significantly in the size and the composition of their carbohydrate components, sensitivity towards sulfhydryl-blocking and protecting reagents, sensitivity to ferric and ferrous ions, thermostability and ability to hydrolyze some nucleotides. The more highly glycosylated form is more sensitive to thermal denaturation. AcPase I and II behave differently towards ascorbate and changes in its concentration and it is suggested that the concentration of reducing modifiers may regulate AcPase activity at the cellular level. It is hypothesized that the differing extents of glycosylation influence the structure of the enzyme forms. This is expressed in altered conformations of two enzyme forms and results in a different exposure of the essential cysteine residues.