Activities and Isozymes of Acid Phosphatase in Schizophyllum commune: A Re-Examination

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Abstract
Specific activities and isozymes of acid phosphatase (AcPase) were analyzed in colonies of Schizophyllum commune, a basidiomycete. Isogenic strains examined included two homokaryons, the dikaryon formed from them, and Bmut, a homokaryon with a primary mutation in the B incompatibility factor. In the homokaryons and the dikaryon AcPase activity increased with age to a peak at nine days and then declined; however, the activity of Bmut continued to rise after the ninth day. Two bands of activity were always present in polyacrylamide gels of extracts from all four strains at all ages analyzed. However, a third band appeared at different times in aging colonies of the homokaryons versus the dikaryon. A plot of the log of the mobility of the isozymes versus gel concentration provided evidence that these isozymes were primarily charge isomers, hence, not likely the result of proteolysis. These results are in contrast to the numerous isozymes of AcPase observed by Wang and Raper for several strains of Schizophyllum. We think their studies contain artifacts produced by the procedures they used.