Purification and Properties of a Yeast Nucleotide Pyrophosphatase

Purification and properties of a yeast nucleotide pyrophosphatase.

A nucleotide pyrophosphatase (EC 3.6.1.9) has been purified from extracts of the hybrid yeast, Saccharomyces fragilis X Saccharomyces dobzhanskii, to an extent where it appears homogeneous by ultracentrifugation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Multiple protein components seen on polyacrylamide and starch gel electrophoresis also exhibit enzyme activity. Ultracentr...

Purification and properties of yeast pyrophosphatase.

Purification of yeast inorganic pyrophosphatase.

An enzyme which hydrolyzes inorganic pyrophosphate (PP) to orthophosphate (ortho P) was demonstrated by Lohmann (1) in muscle. Bauer (2) found that autolysates of slowly dried bottom yeast were a rich source of inorganic pyrophosphatase and were free of adenosinetriphosphatase (ATPase) activity. An important contribution was made by Bailey and Webb (3) who accomplished an extensive purification...

The purification and properties of detergent-solubilized rat liver nucleotide pyrophosphatase.

Nucleotide pyrophosphatase was solubilized from the microsomal fraction of rat liver with Triton X-100 and was purified by ion exchange chromatography on DEAE-cellulose, gel filtration through Sepharose 4B and preparative disc electrophoresis in the presence of 0.1% sodium dodecyl sulfate. This procedure resulted in a final purification of 176-fold. Maintenance of enzymatic activity through the...

Purification and some properties of inorganic pyrophosphatase from human erythrocytes.

Inorganic pyrophosphatase was purified BOO-fold from human erythrocytes by a procedure involving complete hemolysis of the cells, removal of hemoglobin, ammonium sulfate fractionation, diethylaminoethyl cellulose column chromatography, and gel filtration. Magnesium chloride and 2-mercaptoethanol stabilized the activity. The procedure yielded an enzyme with an optimal pH of 7.7, and an apparent ...