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  • 1
    ISSN: 0014-5793
    Keywords: (Cucurbita sp). ; 11 S globulin ; Monensin ; Posttranslational processing ; Protein transport ; Vacuole
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1615-6102
    Keywords: Budding ; Crystalloid ; 11 S globulin ; Protein body ; Pumpkin cotyledon ; Vacuole
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Vacuoles were isolated from pumpkin cotyledons at three developmental stages and judged to be pure by light microscopic inspection and marker enzyme assays. The time sequence of structural changes of vacuoles were examined by light microscopic inspection in parallel with their stainability with neutral red. Vacuoles isolated from the early stage of cotyledon development were heterogeneous in size (Ø=2–10 Μm) but stained uniformly with the dye. In contrast, vacuoles isolated from the middle stage were much larger (Ø=5–15 Μm), and there exist one to three cores, unstainable with neutral red, within a single vacuole. Electron microscopic observation confirms that vacuoles contain a few protein cores in cotyledon cells at the middle stage. Characteristically at this stage, it was observable that some large cores (Ø=4Μm) were budding from vacuoles. At the late stage, size of vacuoles becomes much smaller (Ø=6Μm), nearly equal to that of the protein bodies in dry seeds. Importantly, at this stage most of the volume of each vacuole was occupied by a single core, and only a small matrix space was stainable with neutral red. Suborganellar fractionation indicates that the vacuolar cores were identical to the crystalloids deposited in the protein bodies in dry seeds. Overall results strongly provide the evidence that one crystalloid buds from the vacuole during the later stage of seed maturation, giving rise to a protein body.
    Type of Medium: Electronic Resource
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