Thesis

Neurospora crassa phosphoserine phosphatase : the effect of pH on the hydrolysis of phosphoserine by enzymes present in wild type and ser(JBM-5) extracts and partial purification and characterization of wild type phosphoserine phosphatase

The effect of pH on the hydrolysis of phosphoserine by enzymes extracted from Neurospora crassa was found to be different for wild type than for the serine requiring mutant ser(JBM-5). The pH profile of activity in ser(JBM-5) extracts lacks a shoulder at pH 7.0 which is present in the wild type extracts, while the activity from pH 7.5 to pH 9.5 has the characteristics of alkaline phosphatase and is similar in both mutant and wild type extracts. The presence of a specific phosphoserine phosphatase is indicated by the fact that the hydrolytic activity at pH 7. 0 is not inhibited by Be++ or KCN, both of which are known inhibitors of alkaline phosphatase. Saturated ammonium sulfate fractionation was consistent with two separate specificities.(See more in text)

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