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  • 1970-1974  (4)
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology 25 (1974), S. 167-193 
    ISSN: 0066-4294
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 26 (1972), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A very rapid increase in particulate cytochrome c reductase activity during the very early stages of germination of lettuce is demonstrated. The increase in activity does not parallel water uptake or the increase in cytochrome oxidase activity. The increase is reversible on drying of imbibed seeds and is not inhibited by cyanide. It is concluded that the increase in activity is due to some kind of activation process and not to de novo synthesis of protein. Possible mechanisms of activation were investigated. It was not possible to simulate the activation process in vitro, in the isolated particulate fraction.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 24 (1971), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: At least nine acid phosphatases and a distinct phytase are present in different cell fractions of germinating lettuce. The enzymes could be partially characterised using acrylamide gel electrophoresis. Phosphatase formation is only partially inhibited by cycloheximide. A new soluble ATPase arises between 24 and 48 hours of germination. Its formation is not inhibited by cycloheximide. Phosphatase activity in the particulate fraction of the cell can be liberated and activated by detergent or trypsin treatment. It is suggested that the newly formed soluble ATPase arises by release and activation of a particulate phosphatase.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 25 (1971), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: No evidence could be obtained for hormonal control of amylopectin-l,6-glucosidase activity in germinating peas for the first 72 hours of germination. The embryonic axis did not stimulate the appearance of enzyme activity. The autolytic system which releases amylopectin-l,6-glucosidase activity from the particulate fraction, in which it originates, was studied in greater detail. Using Cu2+ ions to inhibit a proteolytic enzyme in vivo, it was shown that enzyme activation can occur in the zymogen-like granules without liberation of the enzyme into the soluble cell fraction. Activity so formed is labile. Some of the data on proteolytic enzymes in peas is discussed and an attempt made to interpret the liberation of amylopectin-l,6-glucosidase in peas on the basis of the involvement of at least two distinct proteolytic enzymes.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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