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  • 1
    ISSN: 1432-2048
    Keywords: Hordeum (chlorophyll biosynthesis) ; Chlorophyll biosynthesis ; Gene regulation ; Mutant (barley) ; Protochlorophyllide oxidoreductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Components of chlorophyll biosynthesis were investigated in the plastid-ribosome-deficient albostrians mutant of barley (Hordeum vulgare L.). Compared with green leaves, white leaves lacked chloroplast tRNAGlu and 16S ribosomal RNA, but contained a much higher level of the mRNA for glutamate 1-semialdehyde aminotransferase. Substantial amounts of protochlorophyllide were accumulated when the mutant was incubated in a solution of δ-aminolevulinic acid. The level of protochlorophyllide oxidoreductase mRNA (PCOR, EC 1.6.99.1.) in etiolated albostrians plants reached only about 50% of the level in wild-type plants. In addition the content of PCOR protein and the activity of chlorophyll synthetase were distinctly lower than in the wild-type. Mutant and wild-type barley seedlings which were grown under a daily light/dark regime and were therefore nonetiolated both possessed PCOR mRNA. The data presented may help explain the albino phenotype of this mutant. The results are discussed in relation to biosynthesis of tetrapyrrols in higher plants, regulation of chlorophyll biosynthesis and the action of a plastidderived signal involved in the expression of certain nuclear genes.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 135 (1983), S. 30-35 
    ISSN: 1432-072X
    Keywords: Rhodophyta ; Cyanidium caldarium ; Biliprotein ; Levulinic acid ; δ-aminolevulinic acid incorporation ; Phycocyanin apoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cultures of the unicellular red alga Cyanidium caldarium were transferred from heterotrophic growth conditions to photoautotrophic growth. During photoautotrophic growth, the biliprotein phycocyanin is synthesized de novo. In the presence of 2–5 mM/l levulinic acid which inhibits the biosynthesis of tetrapyrrole chromophores, phycocyanin biosynthesis is suppressed by a factor of 29. Immunoprecipitation yields small amounts of “apoprotein” i.e. phycocyanin which lacks all or part of its chromophore(s). In various experiments the ratio apoprotein/residual holoprotein (phycocyanin) was determined as 2–6 to one. Incubation with [3H]leucine leads to labelled immunoprecitable material: apoprotein (18,300–19,600 Mr) and larger poly-peptides (50,000–52,000 Mr) of unknown nature. The apoprotein was separated from residual phycocyanin by chromatography on DEAE-cellulose and preparative isoelectric focusing (IEF). The significance of the results for further studies on the last steps of phycocyanin biosynthesis is discussed.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-5028
    Keywords: Avena sativa L. ; avenacosidase ; β-glucosidases ; BGA family ; defence system ; phytochrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A protein consisting of 60 kDa subunits (As-P60) was isolated from etiolated oat seedlings (Avena sativa L.) and characterized as avenacosidase, a β-glucosidase that belongs to a preformed defence system of oat against fungal infection. The enzyme is highly aggregated; it consists of 300–350 kDa aggregates and multimers thereof. Dissociation by freezing/thawing leads to complete loss of enzyme activity. The specificity of the enzyme was investigated with para-nitrophenyl derivatives which serve as substrates, in decreasing order β-fucoside, β-glucoside, β-galactoside, β-xyloside. The corresponding orthonitrophenyl glycosides are less well accepted. No hydrolysis was found with α-glycosides and β-thioglucoside. An anti-As-P60 antiserum was prepared and used for isolation of a cDNA clone coding for As-P60. A presequence of 55 amino acid residues was deduced from comparison of the cDNA sequence with the N-terminal sequence determined by Edman degradation of the mature protein. The presequence has the characteristics of a stroma-directing signal peptide; localization of As-P60 in plastids of oat seedlings was confirmed by western blotting. The amino acid sequence revealed significant homology (〉39% sequence identity) to β-glucosidases that are constituents of a defence mechanism in dicotyledonous plants. 34% sequence identity was even found with mammalian and bacterial β-glucosidases of the BGA family. Avenacosidase extends the occurrence of this family of β-glucosidases to monocotyledonous plants.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-2048
    Keywords: Hordeum (chlorophyll biosynthesis) ; Chlorophyll biosynthesis ; Gene regulation ; Mutant (barley) ; Protochlorophyllide oxidoreductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Components of chlorophyll biosynthesis were investigated in the plastid-ribosome-deficientalbostrians mutant of barley (Hordeum vulgare L.). Compared with green leaves, white leaves lacked chloroplast tRNAGlu and 16S ribosomal RNA, but contained a much higher level of the mRNA for glutamate 1-semialdehyde aminotransferase. Substantial amounts of protochlorophyllide were accumulated when the mutant was incubated in a solution of δ-aminolevulinic acid. The level of protochlorophyllide oxidoreductase mRNA (PCOR, EC 1.6.99.1.) in etiolatedalbostrians plants reached only about 50% of the level in wild-type plants. In addition the content of PCOR protein and the activity of chlorophyll synthetase were distinctly lower than in the wild-type. Mutant and wild-type barley seedlings which were grown under a daily light/dark regime and were therefore nonetiolated both possessed PCOR mRNA. The data presented may help explain the albino phenotype of this mutant. The results are discussed in relation to biosynthesis of tetrapyrrols in higher plants, regulation of chlorophyll biosynthesis and the action of a plastidderived signal involved in the expression of certain nuclear genes.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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