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  • 1
    ISSN: 1432-2048
    Keywords: Cell-free translation ; Lectin ; Long-lived mRNA ; Pisum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Extracts prepared from dry pea (Pisum sativum, L; cv oberon) primary axes translate efficiently their endogenous messengers in an in vitro protein synthesizing system. The native long-lived messengers are biologically fully active and direct the synthesis of a whole range of polypeptides with MW ranging up to 130,000. About 0.5% of the total in vitro synthesized polypeptides are recovered in the immunoprecipitate obtained with pea lectin antiserum. Since about one-fourth of the radioactivity in the immunoprecipitate comigrates with authentic pea lectin it is concluded that about 0.1% of the long-lived messengers code for the lectin.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Hybrid lectin ; Isolectin ; Lectin ; Triticum (lectins)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wheat (Triticum aestivum) germ agglutinin represents a complex mixture of multiple isolectin forms. Upon ion exchange chromatography at pH 3.8, three isolectins can be separated, each of which is composed of two identical subunits. At pH 5.0, however, three additional isolectins can be distinguished, which are built up of two different subunits (heteromeric lectins). Evidence is presented that these heterodimers are normal constituents of the wheat embryo cells. Analyses of the isolectin patterns in extracts from Triticum monococcum, Triticum turgidum dicoccum and Triticum aestivum, provide evidence that each genome, either in simple or complex (polyploid) genomes, directs the synthesis of a single lectin subunit species. In addition, a comparison of the isolectin pattern in these wheat species of increasing ploidy level, made it possible to determine unequivocally the genome by which the individual lectin subunits in polyploid species are coded for. The possible use of lectins in studies on the origin of individual genoms in polyploid species is discussed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Planta 154 (1982), S. 568-572 
    ISSN: 1432-2048
    Keywords: Heteromeric lectin ; Hordeum ; Lectin ; Secale ; Triticale ; Triticum (lectins)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Lectins from Triticum monococcum, Secale cereale (rye), and Hordeum vulgare (barley) can exchange their subunits in vitro and thereby form (intergeneric) heteromeric lectins. An analysis of the isolectin pattern of a Triticale variety revealed that intergeneric heterodimers of wheat and rye lectin subunits are normal constituents of the embryo cells. It appears, therefore, that these different cereal lectins are structurally so closely related that their subunits can not distinguish between identical and nonidentical partners when they associate into dimers.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Planta 156 (1982), S. 41-44 
    ISSN: 1432-2048
    Keywords: Germination (seeds) ; Lectin ; mRNA (preformed) ; Secale (lectins) ; Seed development ; Triticum (lectins)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wheat (Triticum aestivum L.) and rye (Secale cereale L.) lectins are specifically synthesized during seed formation. They accumulate exponentially in the primary axes in a period coinciding with the development of this complex organ. Since the specific lectin content also increases dramatically, there is apparently an outburst of lectin synthesis during the development of the primary axes. Germinating embryos also synthesize some lectin. The fortunate availability of a highly specific procedure for the isolation of cereal lectins enabled us to follow the kinetics of their synthesis during early germination. Stored mRNAs appear to be involved in this residual lectin synthesis.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Planta 160 (1984), S. 222-228 
    ISSN: 1432-2048
    Keywords: Bryonia ; Lectin ; N-acetylgalactosamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An N-acetylgalactosamine-specific lectin has been isolated from root stocks of Bryonia dioica by affinity chromatography on fetuin-agarose. It is a dimeric protein composed of two different subunits of relative molecular masses 32,000 and 30,000, held together by intermolecular disulphide bonds. Although most abundant in root stocks, the lectin occurs in all vegetative parts of the plant but not in seeds. Bryony lectin differs from other Cucurbitaceae lectins and from all known N-acetylgalactosamine-specific lectins.
    Type of Medium: Electronic Resource
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