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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Applied physics 61 (1995), S. 221-225 
    ISSN: 1432-0630
    Keywords: 78.65 ; 07.75 ; 81.60 ; 82.80
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract In Resonant Laser Ablation (RLA), material is related and selectively ionized by a low-energy pulse from a tunable laser. The selectivity and efficiency allow detection and quantitation at very low concentrations. We demonstrate that RLA has potential use in profiling thin layer and multilayer structures. Quantitative results are reported on the analysis of 20 and 100 Å copper thin films on Si(110) surfaces. Removal rates range from 10−3 to 10−2 Å/shot. Prospects for interrogation of dopants and impurities are also evaluated.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Key words:Brassica ; (sinigrin immunolocalization) ; Glucosinolate ; Myrosinase ; Protein body ; β-Thioglucoside glucohydrolase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Polyclonal rat antibodies were raised to a bovine serum albumin-sinigrin conjugate and used to immunolocalize sinigrin (2-propenylglucosinolate) in imbibed seeds and developing seedlings of Brassica juncea. (L.) Czern. Sinigrin was localized to protein bodies in aleurone-like cells but shown to be absent from myrosin cells. Double labelling techniques were used to co-localize both myrosinase (β-thioglucoside glucohydrolase, EC 3.2.3.1) and sinigrin. Myrosin grains were labelled only with the anti-myrosinase antibody, but aleurone cells were labelled with both anti-myrosinase and anti-sinigrin antibodies. High-performance liquid chromatographic analysis of conventionally fixed and dehydrated seed tissues (4 h post imbibition in water), indicated a high proportion of sinigrin was retained in fixed tissues. Over a time course of 100 h, protein bodies within aleurone-like cells degraded, fused to form the cell vacuole and lost all myrosinase labelling but retained residual sinigrin labelling. The degradation of protein bodies corresponded to a decrease in retention of sinigrin in the fixed tissues. The results describe for the first time the co-localization of a plant enzyme and its substrate, a secondary metabolite.
    Type of Medium: Electronic Resource
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