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  • 1
    Unknown
    NanoBioTechnology : BioInspired Devices and Materials of the Future (2008)
    Totowa, NJ : Humana Press
    Details
    Keywords: Biochemistry ; Biotechnology ; Nanotechnology
    ISBN: 9781597452182
    URL: https://doi.org/10.1007/978-1-59745-218-2
    Language: English
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    E-BOOK
  • 2
    Electronic Resource
    Electronic Resource
    Immobilized endo-.beta.-glucosidase enriches flavor of wine and passion fruit juice (1990)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 38 (1990), S. 1387-1390 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00096a019
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  • 3
    Electronic Resource
    Electronic Resource
    A Clostridium cellulovorans gene, engD, codes for both endo-β-1,4-glucanase and cellobiosidase activities (1990)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 72 (1990), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A 5.8 kbp DNA fragment from Clostridium cellulovorans (ATCC 35296) containing endo-β-1,4-glucanase (1,4-β-d-glucan glucanohydrolase, carboxymethylcellulase, CMCase; EC 3.2.1.4) gene, engD was cloned in Escherichia coli. The clone harboring a subcloned 3.8 kb fragment in plasmid, pEQ52V, produced an enzyme that showed both endo-β-1,4-glucanase activity as well as cellobiosidase activity. Zymograms with the engD encoded enzyme with carboxymethyl-cellulose as the substrate indicated that the molecular mass of the active protein was 50 000.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1990.tb03903.x
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  • 4
    Electronic Resource
    Electronic Resource
    Peroxidase activity associated with suberization processes of the muskmelon (Cucumis melo) rind (2004)
    Oxford, UK; Malden, USA : Munksgaard International Publishers
    Physiologia plantarum 121 (2004), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The rind of fruits of muskmelon (Cucumis melo L. var. reticulatus) contains a network of suberized tissue referred to as the ‘netting’, and peroxidase (EC 1.11.1.7) activity is necessary to the polymerization of the aromatic domain of suberin. Peroxidase activity increased dramatically during the early stages of melon fruit netting, and in fruits exhibiting incomplete netting, peroxidase activity was significantly higher in netted than in non-netted regions of the same fruit. Moreover, analysis of peroxidase activity in three varieties of smooth-rind melons (Cucumis melo var. inodorous) indicated lower levels of the activity in rind samples, taken throughout fruit development, than in rinds of netted varieties. Netting-associated anionic peroxidase (NAPOD) was isolated from the melon rind at an early stage of netting development, partially purified, microsequenced and its cDNA was cloned. It was found to be a single-copy gene within the genome of netted and smooth melon varieties, and highly homologous to other Cucurbitaceous anionic peroxidases. A high transcript level was only detected in the rind of the netted variety. Monitoring the gene expression of netting-associated anionic peroxidase, together with other enzymes involved in the netting will shed light on the molecular control of the suberization processes in the melon rind and in plants in general.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.0031-9317.2004.00301.x
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  • 5
    Electronic Resource
    Electronic Resource
    Differential accumulation of water stress-related proteins, sucrose synthase and soluble sugars in Populus species that differ in their water stress response (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 99 (1997), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Proteins inducible by dehydration and abscisic acid (ABA), have been identified in a number of species and have been suggested to play a role in desiccation tolerance. Recently, we identified a novel boiling-stable protein (BspA) which accumulated in shoots of aspen (Populus tremula L.) cultured in vitro, in response to gradual water stress and ABA application (Pelah et al. 1995. Tree Physiol. 15: 673–678.). Accumulation of BspA, and of the water stress-related protein dehydrin dsp- 16 and sucrose synthase from the resurrection plant. Craterostigma plantagineum, was examined in two greenhouse-grown Populus species to investigate the relationship between the presence of the proteins and water stress tolerance. Detached leaves of Populus tomentosa lost more water than Populus popularis, resulting in a significant decrease in leaf water potential. Using electrolyte leakage analysis, it was found that detached leaves of Populus popularis are more tolerant to water stress than those of Populus tomentosa. Using western blots with the corresponding antibodies, we have found in Populus popularis accumulation of BspA and sucrose synthase due to water stress, and the constitutive presence of a dehydrin-like protein. In contrast, a low expression of BspA was found in Populus tomentosa, but not of sucrose synthase and dehydrin-like proteins. Desiccation tolerance in many tissues can be partly attributed to soluble sugars. Analysis of the amount of soluble sugars did not reveal clear-cut differences between the two species, except for significant sucrose accumulation and glucose reduction in water-stressed Populus tomentosa and increase in glucose in water-stressed Populus popularis. The data obtained points to a positive correlation between increased water stress tolerance of one poplar species as compared with another and accumulation of water stress-related proteins and sucrose synthase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1997.tb03443.x
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  • 6
    Electronic Resource
    Electronic Resource
    Sugars enhance the expression of gibberellin-induced genes in developing petunia flowers (2000)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 109 (2000), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Sugar is essential for the development of detached Petunia hybrida flowers. We have shown that sucrose (Suc) and gibberellic acid (GA3) are required for anthocyanin accumulation and the expression of various genes in developing petunia corollas. The effect of GA3 on the expression of the gibberellin-induced gene and chalcone synthase gene, in detached corollas, was promoted by metabolic sugars such as Suc, glucose (Glc) and fructose, but not by the nonmetabolized 3-O-methylglucose and the sugar alcohol, mannitol. Several pieces of evidence support sugars’ signaling role in the corollas and the possible involvement of hexokinase as the sugar sensor. Mannose, which is inefficiently metabolized but is phosphorylated by hexokinase at efficiency similar to Glc, was as effective as Glc in promoting gene expression and pigmentation. 2-Deoxyglucose, which is a substrate for hexokinase but is not metabolized in glycolysis, also promoted gene expression. On the other hand, mannoheptulose, a competitive inhibitor of hexokinase, completely abolished the promotive effect of Glc. We suggest that sugar-phosphorylation-related signal transduction interacts with the gibberellin signal to induce gene expression and anthocyanin accumulation in developing petunia corollas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.2000.100212.x
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  • 7
    Electronic Resource
    Electronic Resource
    Stigmatic RNase in calamondin (Citrus reticulata var. austera x Fortunella sp.) (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 94 (1995), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In calamondin. which is self-compatible, ribonuclease (RNase) activity was found in the stigmatic diffusate. Tissue print experiments using calamondin styles demonstrated that most of the RNase is localized in the stigma. Stigmatic RNase activity was monitored at different developmental stages of the flower and was found to peak at anthesis. An SDS-PAGE-zymogram indicated the molecular mass of this RNase to be 24 kDa. In vitro germination of calamondin pollen showed a higher percentage of germination in the presence of diffusate from one stigma than in the control. However, diffusates from 3.5 and 7 stigmata per 100 μl aliquots of growth medium, exhibiting 15. 25 and 35 units ml−1 RNase activity, respectively, had successively stronger inhibition effects on the percentage of germination. Diffusate from 7 stigmata inhibited pollen tube elongation, as well as pollen germination. Both the 24-kDa Stigmatic RNase and RNase TI significantly inhibited pollen germination and pollen tube elongation. In pollen tubes treated with either the 24-kDa stigmatic RNase or RNase TI, considerable deposition of callose was observed, as compared to the control which had only a thin callosic cell wall.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1995.tb00971.x
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  • 8
    Electronic Resource
    Electronic Resource
    Cloning and characterization of elongation specific endo-1,4-β-glucanase (cel1) from Arabidopsis thaliana (1997)
    Springer
    Plant molecular biology 34 (1997), S. 837-842 
    Details
    ISSN: 1573-5028
    Keywords: elongation ; gene expression ; glucanase ; Arabidopsis thaliana
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The isolation of an elongation-specific endo-1,4-β-glucanase-cel1 from Arabidopsis thaliana was made possible by the fact that considerable homology exists between different endo-1,4-β-glucanase (EGase) genes from different plants. Degenerate primers were synthesized based on two conserved regions from the avocado and tomato cellulase amino acid sequences. The A. thaliana cel1 cDNA gene was found to encode a 54 kDa protein; sequence comparison with the avocado EGase revealed 56% identity. Northern blot analysis of cel1 suggested its developmental regulation. RNA transcripts were undetectable in fully expanded leaves as well as at the basal internode of flowering stems. However, a strong transcript signal was detected in the elongating zone of flowering stems of normal plants. The RNA transcript level of cel1 in the elongating zone of dwarf flowering stems was significantly lower than in the corresponding zone in normal plants. This suggests cel1's involvement in cell elongation in A. thaliana. Transgenic tobacco plants transformed with the putative cel1 promoter region fused to the gus reporter gene, showed a significant GUS staining both in shoot and root elongating zones. These results further substantiate the link between cel1 expression and plant cell elongation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005849627301
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  • 9
    Electronic Resource
    Electronic Resource
    Analysis of functional domains of endoglucanases from Clostridium cellulovorans by gene cloning, nucleotide sequencing and chimeric protein construction (1992)
    Springer
    Molecular genetics and genomics 231 (1992), S. 472-479 
    Details
    ISSN: 1617-4623
    Keywords: Nucleotide sequence ; Chimeric protein ; Endoglucanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequence of engD, an endo-β-1,4-glucanase gene from Clostridium cellulovorans was determined (Genbank Accession No. M37434). The COON-terminal part of the gene product, EngD, contained a Thr-Thr-Pro repeated sequence followed by a region that has homology to the exoglucanase of Cellulomonas fimi. EngD and EngB, another C. cellulovorans endoglucanase, show 75% amino acid sequence homology at their NH2-termini, in contrast to their carboxyterminal domains which show no homology. EngD had endoglucanase activity on carboxymethylcellulose (CMC), cellobiosidase activity on p-nitrophenyl-cellobioside (p-NPC), and partial hydrolytic activity on crystalline cellulose (Avicel), while EngB showed hydrolytic activity against only CMC. Chimeric proteins between EngB and EngD were constructed by exchanging the non-homologous COOH-terminal regions. Chimeric proteins that contained the NH2-terminus of EngD retained cellobiosidase activity but chimeras with the EngB NH2-terminus showed no cellobiosidase activity. Hydrolysis of crystalline cellulose (Avicelase activity) was observed only with the enzyme containing the EngD NH2-terminus and EngD COOH-terminus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00292718
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  • 10
    Electronic Resource
    Electronic Resource
    Multiple active forms of a novel serine protease from Bacillus subtilis (1990)
    Springer
    Molecular genetics and genomics 221 (1990), S. 486-490 
    Details
    ISSN: 1617-4623
    Keywords: Secretion ; Preproprotein ; C-terminal processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have cloned and sequenced a gene (epr) encoding a novel serine protease from Bacillus subtilis. Several active forms of the enzyme with molecular masses between 40 and 34 kDa were found in the medium of B. subtilis cultures containing the epr gene cloned on a plasmid. Deletions at the 3′ end of the gene, removing up to 240 amino acids of the reading frame, abolished the expression of the larger species but did not affect the expression of the 34 kDa enzyme. The C-terminal third of the protein is therefore not required for protease activity. The size variation of the active forms expressed by the complete epr gene appears to be the result of partial removal of the C-terminus either by processing or degradation. Thus, the epr gene consists of two domains, one encoding a serine protease homologous to subtilisin and the other a C-terminus of unknown function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00259415
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