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  • 1
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology 36 (1985), S. 441-472 
    ISSN: 0066-4294
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    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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  • 3
    ISSN: 1615-6102
    Keywords: β-amylase ; Barley endosperm ; Bound β-amylase ; Free β-amylase ; Seed desiccation ; Starch granules
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Association of β-amylase with starch granules in the starchy endosperm of barley (Hordeum vulgare L. cv. Menuet) grains was characterized biochemically. In whole homogenates of dry seeds, two forms of β-amylase were detected: one is free β-amylase extractable with saline solution and the other is bound β-amylase extractable with saline solution containing a reducing agent. The two forms of β-amylase were shown to be identical in terms of mobility on disc gels, antigenicity, and molecular specific activity, indicating that the β-amylase molecules of the two forms are identical. The starch granules were isolated from either dry seeds or mature seeds harvested before the desiccation phase. Both starch granule preparations were morphologically identical by microscopic inspection. The bound β-amylase was predominantly associated with starch granules isolated from dry seeds, whereas it was not associated with starch granules from mature seeds harvested before desiccation. Overall results show that the periphery of starch granules is the major site of deposition for bound β-amylase in dry seeds. The association of β-amylase with starch granules occurs during the desiccation phase of seed development, resulting in the conversion of free β-amylase into a bound form.
    Type of Medium: Electronic Resource
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