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. 1997 Jul 14;138(1):37–44. doi: 10.1083/jcb.138.1.37

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Precursor API is trapped within a vesicle in cvt17 mutants. (A) Precursor API is in a protease-protected compartment in cvt17 mutants. THY32 (cvt17) spheroplasts were subjected to differential lysis and protease treatment in PS200 buffer as in Fig 3. (B) Precursor API is not free in the vacuolar lumen in cvt17 mutants. Differential fractionation was continued by resuspending the P₂₀₀ fraction in PS0 buffer and separating the supernatant (S₀) and pellet (P₀) fractions by centrifugation at 10,000 g. The S₀ and P₀ fractions were treated with proteinase K in the presence and absence of Triton X-100 as indicated. All fractions were precipitated with 10% TCA and resolved by SDS PAGE; proteins of interest were detected by Western blotting. The positions of prAPI, mAPI, and mPrA are indicated.