Enzyme activities during early ascosporulation in Saccharomyces cerevisiae

Ota, Akinobu

doi:10.1016/0020-711x(82)90150-1

International Journal of Biochemistry

1982

DOI: 10.1016/0020-711x(82)90150-1

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Enzyme activities during early ascosporulation in Saccharomyces cerevisiae

Akinobu Ota

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Cited by 5 publications

References 67 publications

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Purification and properties of dipeptidase from Escherichia coli AJ005

Ota

1986

Mol Cell Biochem

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A Co2+-dependent dipeptidase from E. coli strain AJ005, a peptidase-deficient mutant, was purified with streptomycin sulfate, ammonium sulfate and DEAE-cellulose. The purified dipeptidase increased by about 106-fold in specific activity, with dilysine as a substrate. The dipeptidase cleaved dilysine to two lysines among the lysine homopolymers, the possibility remaining that it is active toward peptides other than dilysine, since it was investigated in the present study only for activity toward lysine homopolymers. Activity was inhibited 54% by 10(-3) M KCN and completely by 10(-3) M PCMB, EDTA and benzethonium chloride, but not at all by soybean trypsin inhibitors. 78% and 95% of its activity was lost with 30 minutes' treatment at 45 degrees C and 50 degrees C, respectively. The apparent Km value was 6.7 X 10(-4) M for dilysine. It is probable that the dipeptidase differs from dipeptidase DP.

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Purification and properties of dipeptidase from Escherichia coli AJ005

Ota

1986

Mol Cell Biochem

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Some properties of glucose uptake activity during early ascosporulation in Saccharomyces cerevisiae

Ota

1985

International Journal of Biochemistry

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Some properties of ATPase activity in the intact cells of yeast Saccharomycopsis fibuligera

Ota

Morishita²

1986

International Journal of Biochemistry

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Enzyme activities during early ascosporulation in Saccharomyces cerevisiae

Cited by 5 publications

References 67 publications

Purification and properties of dipeptidase from Escherichia coli AJ005

Purification and properties of dipeptidase from Escherichia coli AJ005

Some properties of glucose uptake activity during early ascosporulation in Saccharomyces cerevisiae

Some properties of ATPase activity in the intact cells of yeast Saccharomycopsis fibuligera

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