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  • 1985-1989  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Development of maize plants from cultured shoot apices (1988)
    Springer
    Planta 175 (1988), S. 9-12 
    Details
    ISSN: 1432-2048
    Keywords: Organ culture ; Shoot apex ; Zea (cultured shoot apex)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Excised shoot apices of maize (Zea mays L.), comprising the apical meristem and one or two leaf primordia, have been cultured and can form rooted plantlets. The plantlets, derived from meristems that had previously formed 7–10 nodes, develop into mature, morphologically normal plants with as many nodes as seed-grown plants. These culture-derived plants exhibited the normal pattern of development, with regard to the progression of leaf lengths along the plant and position of axillary buds and aar shoots. Isolation of the meristem from previously formed nodes reinitiates the pattern and number of nodes formed in the new plant. Thus, cells of the meristem of a maize plant at the seedling stage are not determined to form a limited number of nodes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00402876
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Activation of low and null activity isozymes of maize alcohol dehydrogenase by antibodies (1987)
    Springer
    Molecular genetics and genomics 208 (1987), S. 271-278 
    Details
    ISSN: 1617-4623
    Keywords: ADH ; Enzyme activation ; Isozyme ; Antibody ; Maize
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Antisera were raised against several purified, high specific acitivity isozymes of maize alcohol dehydrogenase (ADH1). The various antisera had different effects on the activity of immunoprecipitated ADH. One antiserum completely inactivated maize ADH. This inactivation could be blocked by preicubation of the enzyme with NAD+, its cofactor, or with NADP. The different antisera were used to analyze variant froms of ADH1. Isozymes having lowered specific activity were activated to wild-type levels by precipitation of the enzymes with noninactivating antisera. Isozymes having no detectable ADH activity (CRM+ nulls) were activated by immunoprecipition with noninactivating antisera when preincubated with NAD+ or NADP. All of the CRM+ nulls were shown to be unable to bind NAD+, a flaw which can account for their lack of activity. The results indicate that a conformational equilibrium between active and inactive forms of maize ADH in solution controls the specific activity of the various isozymes. Both controls the specific activity of the various isozymes. Both NAD+ and antibodies raised against high specific activity enzymes can interact with low activity isozymes to shift the balance of the equilibrium toward the active form, thus increasing their specific activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330453
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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