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- W2030484588 abstract "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." @default.
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- W2030484588 date "1984-01-01" @default.
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- W2030484588 title "Immounological studies on the synthesis of yeast repressible acid phosphatase in the presence of tunicamycin." @default.
- W2030484588 doi "https://doi.org/10.1271/bbb1961.48.1205" @default.
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