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  • 1
    Electronic Resource
    Electronic Resource
    Chloroplast DNA reassociation and grass phylogeny (1991)
    Springer
    Plant systematics and evolution 176 (1991), S. 21-31 
    Details
    ISSN: 1615-6110
    Keywords: Angiosperms ; Poaceae ; Systematics ; phylogeny ; chloroplast DNA reassociation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sequence variation in chloroplast DNA (cpDNA) as measured by DNA reassociation was examined in 12 grass species to address systematic problems in thePoaceae at the subfamilial and tribal levels. Two species,Petunia (Solanaceae) andGlycine (Leguminosae), were included to determine degrees of sequence divergence in cpDNA between monocots and dicots. The data were analyzed phenetically and phylogenetically. Species were segregated into four major groups that corresponded to the subfamiliesPooideae, Oryzoideae, Chloridoideae, andPanicoideae. Representatives of thePooideae andOryzoideae grouped together as did members of theChloridoideae andPanicoideae. ThePooideae split into two major groups corresponding to the recently recognized supertribesTriticanae andPoanae. Internodes between subfamily branches were short which might indicate a burst of divergence in the family early in its evolution. Sequence similarity values between the monocot grass species and the two dicot taxa ranged from 0.15 to 0.27, representing the highly conserved sequences of the chloroplast genome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00937943
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Interactions of proteins with uniform colloidal hematite and chromium hydroxide particles. I. Adsorption (1992)
    Springer
    Colloid & polymer science 270 (1992), S. 353-363 
    Details
    ISSN: 1435-1536
    Keywords: Adsorption ofproteins ; albumin ; chromiumhydroxide ; γ-globulin ; hematite ; lysozyme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract The adsorption of ovalbumin, γ-globulin, and lysozyme on uniform spherical hematite and chromium hydroxide particles in aqueous media has been studied as a function of the pH at a constant ionic strength. The uptake of ovalbumin and γ-globulin was greatest at their isoelectric points and differed little at 10−2 and 10−3 mol dm−3 NaNO3. The adsorption of lysozyme was strongly influenced by the ionic strength. The deposition of ovalbumin on hematite in the presence of Mg (NO3)2 was significantly greater than that with NaNO3 under otherwise comparable conditions. Dialysis experiments with ovalbumin against magnesium nitrate solutions showed Mg2+ to be specifically bound to the protein. The shapes of isotherms indicated monolayer coverage for ovalbumin and multilayer coating for lysozyme for both adsorbents. The shapes of isotherms of γ-globulin on hematite point to a rearrangement of the protein on the particle surface, while a monolayer was found on chromium hydroxide particles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00655850
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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