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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 14 (1976), S. 619-634 
    ISSN: 1573-4927
    Keywords: peptidases ; Zea mays ; isozymes ; gene products
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A number of biochemical properties have been investigated for both allelic and nonallelic forms of maize peptidases. Four aminopeptidases exist in maize (LAP-A, LAP-B, LAP-C, and LAP-D) and are the products of four diallelic loci. The aminopeptidases fall into two biochemical groups on the basis of these studies. LAP-A and LAP-D have comparatively low apparent K m (K app) values for arginine-naphthylamide derivatives and high velocities for arginine-naphthylamide and lysine-naphthylamide. LAP-B and LAP-C, on the other hand, have lower K app values for leucine-naphthylamide and higher velocities for nonpolar amino acid-naphthylamides than for arginine-naphthylamide. LAP-A and LAP-D are also relatively more heat stable than LAP-B and LAP-C and have somewhat higher molecular weights (71,500) than LAP-B and LAP-C (63,500). In determining molecular weights of the peptidases, use was made of their differential substrate specificities toward amino acid-naphthylamides. Some properties of genetically defined maize endopeptidase are also presented. Maize endopeptidase is inhibited by the sulfhydryl reagents N-ethylmaleimide and p-chloromercuribenzoate (pCMB), and by tosyl lysine chloromethyl ketone. Maize aminopeptidase activity is inhibited by N-ethylmaleimide, pCMB, and EDTA (ethylenediamine tetraacetic acid).
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 3 (1982), S. 7-23 
    ISSN: 0192-253X
    Keywords: gene expression ; superoxide dismutase ; Zea mays ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Immunoassays for the cytosolic and mitochondrial superoxide dismutases (SOD) of maize were developed and used to study the expression of these proteins in the maize seedling. The genetically distinct proteins, SOD-3 and SOD-4, are preferentially expressed in the scutellum, comprising approximately 1% of the total water-soluble protein of that tissue. SOD-2, SOD-3, and SOD-4 are synthesized in the scutellum during early sporophytic development, probably on cytosolic ribosomes. Two-dimensional gel electrophoresis of crude scutellar extracts indicates that significant changes occur in the protein composition of the maize scutellum following seed imbibition. Using the immunoassays, a maize line exhibiting a significant reduction in cyanide-sensitive SOD protein was identified.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 4 (1983), S. 99-115 
    ISSN: 0192-253X
    Keywords: differential allelic expression ; Zea mays ; isozyme ; endosperm ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The timing of gene expression in the endosperm of developing F1 maize kernels was investigated. Zymogram analysis revealed the presence of maternally derived allelic gene products on all days investigated, but activity of paternally derived allelic gene products is not detectable until days 6-8 postpollination, depending on the particular cross used and the enzyme investigated. This pattern holds true for eight different isozymes of five different enzyme systems, including catalase, alcohol dehydrogenase, glutamate-oxaloacetate transaminase, endopeptid́ase, and aminopeptidase. An increase in specific activity for catalase, alcohol dehydrogenase, and endopeptidase correlates precisely with the day of visualization of the paternally derived allelic gene product on the zymograms. Rocket immunoelectrophoresis confirms a dramatic increase in catalase and alcohol dehydrogenase protein levels on the day the paternally derived allelic gene product is first detected on zymograms. Appropriate crosses utilizing three different allelic variants revealed the presence of enzyme of maternal plant origin within the endosperm prior to day 6 postpollination.Maize kernels were cultured in vitro on an agar-based medium as early as 3 days postpollination. Using medium supplemented with actinomycin D or cycloheximide, it was possible to localize the critical time periods for transcription and translation of the paternally derived allele in the F1 hybrids. For aminopeptidase (AMP-1, AMP-3) and endopeptidase (ENP-1), transcription occurs as early as 3-4 days postpollination, and translation of the transcripts starts at about 4-5 days postpollination. Although the evidence is indirect, it is likely that the maternally derived allele of the F1 kernels is activated (ie, begins transcribing) synchronously with the paternally derived allele during this early developmental time period.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 12 (1991), S. 423-430 
    ISSN: 0192-253X
    Keywords: Zea mays ; superoxide dismutase ; differential gene expression ; stem lignification ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The temporal and spatial patterns of expression of the Cat and Sod genes encoding the multiple catalases and superoxide dismutases in maize have been examined throughout stem development. Three stages of stem development have been defined based upon catalase activity profiles and stem internode elongation. At stage 1, catalase activity is low and internodes remain short; at stage 2, catalase activity dramatically increases and internodes rapidly elongate; and at stage 3, catalase activity decreases to levels intermediate to stage 1 and 2, and internode elongation ceases. Zymogram analysis and immunoassays show that only the CAT-3 catalase isozyme is present in the stem, even though both Cat1 and Cat3 mRNAs accumulate throughout stem development. Cat2 mRNA is not detectable in the developing stem. In full-grown stems catalase is localized primarily in the sclerenchyma beneath the epidermis and around the vascular bundles and may possibly play a role in lignification. Unlike catalase, all the superoxide dismutase (SOD) isozymes and transcripts are present in the developing stem. Thus, these two major antioxidant gene-enzyme systems show differential patterns of expression during stem development in maize. © 1992 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0192-253X
    Keywords: temporal-regulatory gene ; alcohol dehydrogenase ; gene regulation ; recessive trans-acting gene ; Zea mays ; developmental program ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The developmental program of alcohol dehydrogenase (ADH) activity in the scutellum of maize strain R6-67 is different from that of W64A. The level of scutellar ADH activity in R6-67 remains relatively high during the course of early sporophytic development as compared to the commonly observed pattern. In the typical inbred strain W64A, the activity of ADH declines substantially during that period. The variance values from the crosses between R6-67 and W64A reveal that the trait is under genetic control. Detailed genetic analysis suggests that a single gene is responsible for the altered developmental program of ADH activity in R6-67. This gene meets the criteria for temporal regulatory genes and is different from Adh2, the structural gene which codes the ADH-2 isozyme. We have designated this gene as Adr1 (alcohol dehydrogenase regulator, #1). Adr1 is unlinked to Adh2. There is no de novo synthesis of ADH in the scutellum during germination, and the difference in the activity level reflects the difference in the amount of enzyme protein as demonstrated by density labeling and rocket immunoelectrophoresis. Thus, it appears that Adr1 may regulate the degradation of ADH.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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