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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 2269-2275 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 21 (1949), S. 530-530 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology 20 (1969), S. 495-522 
    ISSN: 0066-4294
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 8 (1960), S. 481-482 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 197 (1963), S. 263-265 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE enzyme nitrate reductase is of major importance A in the nitrogen metabolism of maize1-*. Evidence from earlier work in our laboratory1-2 suggested that it may be significantly involved in grain-yielding capacity, and also established1 that the activity of nitrate reductase is drastically ...
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-2048
    Keywords: Aminopeptidases ; Carboxypeptidases ; Endopeptidases ; Germination (seeds) ; Proteases ; Seedling development ; Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Profiles of pH dependence and activities of live proteolytic enzymes, amino- and carboxypeptidase and endopeptidases active at pH 3.8, 5.4 and 7.5, with casein as substrate, were determined in crude extracts from the various organs of corn seedlings during germination and early development (30°C, dark, 8 d). With respect to the endopeptidases, caseolytic activities at pH 3.8, 5.4 and 7.5 in extracts from endosperm increased concurrently with loss of endosperm N during germination; however, the relative amounts of the pH 7.5 activity were very small. In scutellum extracts, caseolytic activities at both pH 5.4 and 7.5 increased during the initial stages of development but only the increase at pH 5.4 was concurrent with loss of scutellar N. In shoot extracts, caseolytic activities at pH 5.4 and 7.5 were very low and remained relatively constant. There was a progressive increase in shoot N with time. In root extracts, caseolytic activities at pH 5.4 and 7.5 were higher (3-fold) than in shoot extracts. The activity at pH 5.4 remained constant while the activity at pH 7.5 increased during germination. The rate of accumulation of N by the root was low after day 5. The pattern and ratio but not the amounts of the pH 5.4 and 7.5 caseolytic activities of the root were similar to those observed in senescing leaves of field-grown corn. Addition of mercaptoethanol increased (several-fold) the caseolytic activities at pH 3.8 and 5.4, especially the latter, but not the pH 7.5 activity in endosperm extracts and increased the pH 5.4 activity in extracts from scutellum (30%) and roots (30%) while the effect in shoot extracts was negligible. Carboxypeptidase activity was relatively low in young tissue (root tip, 3-d-old shoots) and increased with development of the various organs except the roots (whole) where the activity remained relatively constant. The increases in carboxypeptidase activities were concurrent with decreases in N from endosperm and scutellum; this result indicates that this enzyme in these tissues may be involved (cooperatively with endopeptidases) in the mobilization of reserve protein. Of all the enzymes tested, only carboxypeptidase activity was markedly (in excess of 50%) inhibited by phenylmethylsulfonylfluoride. Only aminopeptidase activity was found in appreciable amounts in endosperm and scutellum of dry kernels. Aminopeptidase activity was highest in organs with high metabolic activity (scutella, shoot, root tips) and decreased in plant parts undergoing rapid loss of nitrogen (endosperm, senescing leaves).
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Nitrite reductase from corn scutellum-a non-chlorophyllous tissue-can use methyl viologen, benzyl viologen or ferredoxin as electron donor. Little or no reduction occurs with nicotinamide or flavin nucleotides. Activity is inhibited by p-chloromercuribenzoate and by cyanide. Organic chelates, with the exception of bathocuproine disulphonate and bathophenanthroline disulphonate, are not inhibitory. Ammonia is the reaction product. Ion exchange chromatography resolves the nitrite reductase activity into two peaks with apparently represent two forms of the enzyme. Both have a molecular weight of 61–63000 as determined by molecular exclusion chromatography, and a pH optimum of 6.7–6.8. Although their properties are generally similar, they show a marked difference in thermal stability, ionic charge and behaviour during isoelectric focusing. Nitrite reductase is found largely in the soluble fraction although some particulate activity is also obtained. Both forms of the enzyme are present in the soluble and particulate fractions.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 193 (1962), S. 247-250 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE reduction of nitrate and its assimilation to ammonia by higher plants depends on several factors, including light1-3, mineral elements2'4-6 and source of nitrogen supply2'6. A metabolic pathway was suggested by Meyer and Schultze in 1894 7 to be NO 3 -〉 NO2 -* H2N2O2 -〉 HONH2 -〉 NH3. ...
    Type of Medium: Electronic Resource
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