Acid phosphatase from needles of Pinus silvestris L. Purification of two interconvertible enzyme forms and characterization of a low-molecular weight factor associated with the enzyme.
Two main forms of acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) have been isolated from needles of Pinus silvestris L. The isoelectric points determined by isoelectro-focusing are 3.6 and 9.4. The molecular weights of both forms were estimated as 68 000. The two forms have similar kinetic properties. Chromatography of the acidic enzyme form on DEAE-cellulose results in conversion to the basic form. Interconversion in the reverse direction was demonstrated to occur on incubation of the basic enzyme form with a pine-needle homogenate or with a low-molecular weight fraction thereof. These findings suggest that the interconvertibility between the main enzyme forms is a result of an association of the basic form with a low-molecular weight factor carrying multiple negative changes. This factor has been purified and tentatively identified as an oligoribonucleotide or a fragment of RNA. The implications of these findings for the application of acid phosphatase isoenzymes as genetic markers in forest trees are discussed.
D000135:Acid Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D002848:Chromatography, DEAE-Cellulose; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D009843:Oligoribonucleotides / Q000302:isolation & purification; D014197:Trees
D007527:Isoenzymes; D009843:Oligoribonucleotides; D000135:Acid Phosphatase