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  • 1
    Electronic Resource
    Electronic Resource
    Cold-shock induction of a family of TIP1-related proteins associated with the membrane in Saccharomyces cerevisiae (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 15 (1995), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: TIP1 is the first known cold-shock-and heat-shock-induced gene in Saccharomyces cerevisiae. Here it is demonstrated that a TIP1 homologue, TIR1, which had been previously cloned as SRP1 (serine-rich protein), is strongly induced by a downshift in growth temperature from 30 to 10°C. We further cloned TIR2, which is transcribed at a low basal level but is increased strongly by cold shock and, to a lesser extent, by heat shock. The predicted protein sequence of TIR2 demonstrates remarkable homology to T1R1 (72.2%) and is also homologous with TIP1 (49%). TIP1, TIR1 and TIR2 are rich in both serine and alanine residues and each contains serine-rich tandem repeats. The proteins contain putative N-terminal signal peptides as well as hydro-phobic C-terminal sequences, indicating that the proteins may be membrane bound. The predicted protein sequences are also consistent with extensive O-mannosylation as well as glycosyl-phosphatidyl inositol (GPI) membrane anchoring. Cell fractionation analysis as well as studies using a yeast strain that is conditionally deficient in glycosylation demonstrate that TIP1 is a heavily modified membrane-associated protein. Single, double combinations and triple mutants were created and none demonstrated any obvious phenotype, indicating that this family of genes is not essential for normal growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1995.tb02248.x
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  • 2
    Electronic Resource
    Electronic Resource
    Low prevalence of clinicopathologic and sialographic changes in salivary glands of men with Sögren's syndrome (1999)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 28 (1999), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Sjögren's syndrome (SS) is uncommon in men and there are few reports that describe their clinical features. In the present study, we investigated salivary gland manifestations in men with SS and compared the results with those in women patients. This study included 12 men and 117 women with SS, and the mean stimulated parotid flow rate in men (4.1 ml/5 min, n=10) was higher than that of the women (3.1 ml/5 min, n=10). The prevalence of SS-related sialographic findings, such as globular and punctate sialectasis, was significantly (P 〈 0.05) lower in men (3/11) than in women (72/117). The prevalence of grade 4 cases on labial salivary gland biopsy was also significantly (P 〈 0.01) lower in men (4/11) than in women (82/111). These results indicate a lower prevalence of SS-related clinicopathologic and sialographic changes in men with SS than in women with the same condition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1999.tb02046.x
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  • 3
    Electronic Resource
    Electronic Resource
    High-level expression of a sweet protein, monellin, in the food yeast Candida utilis (1997)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 15 (1997), S. 453-457 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] We describe the heterologous expression of monellin in the yeast Candida utilis. A single-chain monellin gene was expressed under the control of the glyceraldehyde-3-phosphate decarboxylase gene promoter from C. utilis. A promoter-deficient marker gene allowed high-copy-number integration of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0597-453
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  • 4
    Electronic Resource
    Electronic Resource
    Heat-induced Gelation of Chicken Gizzard Myosin (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 59 (1994), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Chicken gizzard myosin solution formed a gel when heated above 40°C. The rigidity of the gel was constant above 65°C. Maximum pH for gel formation was 5.9 at 0.6M and 5.7 at 0.15M KCl. Higher rigidity of the myosin gel was observed at low ionic strength than at high ionic strength. Rigidities of myosin at 0.6M KCl increased by (mg/mL)2.5 and at 0.15M (mg/mL)1, 4 myosin concentration. The strength of gizzard myosin gels was comparable to that of myosin gels from chicken breast muscle under similar conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1994.tb08112.x
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation and functional identification of a novel cDNA for astaxanthin biosynthesis from Haematococcus pluvialis, and astaxanthin synthesis in Escherichia coli (1995)
    Springer
    Plant molecular biology 29 (1995), S. 343-352 
    Details
    ISSN: 1573-5028
    Keywords: astaxanthin ; canthaxanthin ; carotenoid ; xanthophyll ; Haematococcus pluvialis ; green alga
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We succeeded in isolating a novel cDNA involved in astaxanthin biosynthesis from the green alga Haematococcus pluvialis, by an expression cloning method using an Escherichia coli transformant as a host that synthesizes β-carotene due to the Erwinia uredovora carotenoid biosynthesis genes. The cloned cDNA was shown to encode a novel enzyme, β-carotene ketolase (β-carotene oxygenase), which converted β-carotene to canthaxanthin via echinenone, through chromatographic and spectroscopic analysis of the pigments accumulated in an E. coli transformant. This indicates that the encoded enzyme is responsible for the direct conversion of methylene to keto groups, a mechanism that usually requires two different enzymatic reactions proceeding via a hydroxy intermediate. Northern blot analysis showed that the mRNA was synthesized only in the cyst cells of H. pluvialis. E. coli carrying the H. pluvialis cDNA and the E. uredovora genes required for zeaxanthin biosynthesis was also found to synthesize astaxanthin (3S, 3′S), which was identified after purification by a variety of spectroscopic methods.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00043657
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  • 6
    Electronic Resource
    Electronic Resource
    Cloning and sequence analysis of the arginine deiminase gene from Mycoplasma arginini (1990)
    Springer
    Molecular genetics and genomics 221 (1990), S. 81-86 
    Details
    ISSN: 1617-4623
    Keywords: Mycoplasma arginini ; Arginine deiminase ; Molecular cloning ; Nucleotide sequence ; Codon usage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Arginine deiminase from Mycoplasma arginini was purified. The purified enzyme has a molecular weight of 46000 daltons as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Its specific activity (20 units/mg protein) and amino acid composition showed a strong similarity to that of the Mycoplasma arthritidis arginine deiminase. The amino acid sequences of the N-terminal region and three internal peptides generated by enzymatic cleavage of the purified protein were determined. Using a synthetic oligonucleotide mixture complementary to part of the determined N-terminal amino acid sequence, the gene coding for arginine deiminase was isolated from a phage library. A nucleotide sequence of 2189 by encoding the gene was determined. An open reading frame (ORF) contained the amino acid sequences corresponding to the determined N-terminal region and the three internal peptides of arginine deiminase. Thus it was concluded that this ORF encoded the arginine deiminase, a 385 amino acid polypeptide (mol.wt. 43900 daltons). The three tryptophan residues in the sequenced peptides align with UGA codons in the nucleotide sequence, indicating that the nonsense codon UGA is used as a tryptophan codon in M. arginini.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00280371
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  • 7
    Electronic Resource
    Electronic Resource
    Production of lycopene by the food yeast, Candida utilis that does not naturally synthesize carotenoid (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 58 (1998), S. 306-308 
    Details
    ISSN: 0006-3592
    Keywords: lycopene ; Candida utilis ; carotenoids ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The Erwinia uredovora crtE, crtB, and crtI genes, which are responsible for the synthesis of carotenoid lycopene from farnesyl pyrophosphate, were expressed in Candida utilis under the control of the promoters and terminators derived from the C. utilis GAP, PGK, and PMA genes, respectively. The yeast transformant carrying the carotenoid biosynthesis genes produced 758 μg/g dry weight of lycopene along with 407 μg/g dry weight of phytoene in the stationary phase. It was observed in the C. utilis transformant that ergosterol content was decreased to 65% of that in the parent strain that accumulated 6.04 mg/g dry weight of ergosterol. It is therefore possible that the carbon flux for the ergosterol biosynthesis has been branched at farnesyl pyrophosphate to generate a new pathway for the lycopene production in this yeast transformant. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 58:306-308, 1998.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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