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  • Blackwell Publishing Ltd  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of the World Aquaculture Society 32 (2001), S. 0 
    ISSN: 1749-7345
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Conadal production was studied in Loxechinus albus (Molina, 1782) maintained in cages suspended from a long-line in the Estero Castro, Chiloé for 3 mo during the austral summer. The sea urchins were fed either an artificial diet or a natural diet consisting of the macroalgae Macrocystis pyrifera and Ulva sp. Both diets were tested for four size ranges: 40–45, 50–55, 60–65 and 70–75 mm diameter. For all four size ranges, highest gonad production was with the artificial diet. Gonad production was greatest in the 40–45 mm individuals with an increase of about 1,400% and 750% in the wet weight of gonads in individuals fed the artificial and natural diet, respectively. With the three other size ranges, the increase was nearly 100% with the artificial diet and nearly 0% with the natural diet The gonad index showed similar patterns, being highest in the smallest individuals. Small individuals fed the artificial diet would provide the most cost effective aquaculture as production is best. It is not necessary to grow L. albus to the minimal legal size for fisheries (70-mm diameter) for cost effective gonad production.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of the World Aquaculture Society 28 (1997), S. 0 
    ISSN: 1749-7345
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Loxechinus albus were fed algae (Macrocystis pyrifera and Ulva sp.) and two feeds prepared by extrusion (one containing kelp). Results were the same for individuals maintained in suspended cages in the sea and in aquaria on land. Gonads increased in size in individuals fed extruded feeds and decreased in individuals fed algae during the spawning season. Gonads increased ca. four-fold in size in individuals fed the extruded feeds during the post-spawning season, much greater than those fed algae. Individuals fed extruded feeds had a lower feeding rate than individuals fed algae on a wet-weight but not on a dry-weight basis. The extruded feed supports gonadal growth more than natural food and has potential for use for aquaculture of sea urchins.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract Western blot analysis (immunoblotting) of cell surface-associated proteins from Helicobacter pylori confirmed our previous findings that binding of human IgG is a common property (among H. pylori strains). Purification of the IgG-binding proteins (IGBP) was achieved by two purification steps, affinity chromatography on IgG-Sepharose and nickel chelate affinity chromatography. SDS-PAGE and immunoblotting analysis revealed a 60 kDa protein with affinity for peroxidase labeled human IgG. Solid phase binding assays showed that IgG binds to an immobilized protein (IGBP). The 60 kDa IGBP binds human IgG1, IgG3 and IgM. Binding could be inhibited by the kappa chain of the human IgG, but not with its Fc fragment, nor with IgA or IgM. In addition, rabbit polyclonal antibodies raised against the 60 kDa IGBP blocked IgG binding. Monoclonal antibodies, specific to the Hsp60 heat shock protein of H. pylori recognized the 60 kDa IGBP as revealed by immunoblotting analysis, both in crude preparations and in the purified fractions.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 16 (1996), S. 0 
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract Bovine lactoferrin binds to a 60 kDa heat shock protein of Helicobacter pylori. Binding ability was related to human immunoglobulin G because bovine lactoferrin binding proteins were isolated by extraction of cell surface associated proteins with distilled water, applied on IgG-Sepharose and nickel sulphate chelate affinity chromatography. Binding was demonstrated by Western blot after purified protein was digested with α-chymotrypsin and incubated with peroxidase-labeled bovine lactoferrin. Binding was inhibited by bovine lactoferrin, lactose, rhamnose, galactose, and two iron-containing proteins, ferritin and haptoglobin. Helicobacter pylori binds ferritin and haptoglobin via charge or hydrophobic interactions because this binding was not inhibited by specific and various glycoproteins or carbohydrates. Carbohydrate moieties of bovine lactoferrin molecules seem to be involved in binding because glycoproteins with similar carbohydrate structures strongly inhibited binding. Scatchard plot analysis of the binding of peroxidase-labeled bovine lactoferrin to H. pylori cells yielded a kd 2.88 × 10−6 M. In addition, binding of H. pylori cells to bovine lactoferrin was enhanced when bacteria treated with pepsin or α-chymotrypsin after isolation from iron-restricted and iron-containing media.
    Type of Medium: Electronic Resource
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