Immunological Studies on the Synthesis of Yeast Repressible Acid Phosphatase in the Presence of Tunicamycin

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概要

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• When yeast protoplasts that were producing repressible acid phosphatase (r-APase) were treated with tunicamycin (TM), three specific proteins of 59k, 57k, and 55k daltons were accumulated in the membrane fraction in addition to the usual membrane proteins and these proteins were not detected in the secreted fraction. These proteins were immunoprecipitated with anti r-APase antiserum. Their molecular sizes were almost the same as those endo-H treated r- APase. Therefore these proteins were considered to be nonglycosylated forms of r-APase proteins. These results proved that nonglycosylated forms of r-APase produced by TM-treatment were not secreted by yeast protoplasts.

• 社団法人 日本農芸化学会の論文

著者

• MIZUNAGA Takemitsu

  Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo

• NOGUCHI Toshihiro

  Department of Agricultural Chemistry, The University of Tokyo

• MARUYAMA Yoshiham

  Department of Agricultural Chemistry, The University of Tokyo

• MIZUNAGA Takemitsu

  Department of Agricultural Chemistry, The University of Tokyo

関連論文

• The Presence of Protein Disulfide Isomerase in the Yeast Saccharomyces cerevisiae(Biological Chemistry)
• Immunological Studies on the Synthesis of Yeast Repressible Acid Phosphatase in the Presence of Tunicamycin
• Function of MannanChains of Yeast Repressible Acid Phosphatase on Its Enzymatic Properties

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