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  • 1980-1984  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 7 (1980), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: α-Galactosyltransferase which participates in the biosynthesis of blood group B substance was found in urine from group B and AB healthy persons of both secretors and non-secretors.The activity of α-galactosyltransferase in the urine of healthy variant Bm person was lower than that found in a normal group B person. This enzyme in urine of A1Bm persons must be much lower than that in normal AB persons. Its activity was not detected by the method of group O to group B transformation of erythrocytes.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 7 (1980), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: α-L-Fucosyltransferases were demonstrated in human saliva which catalyze the transfer of L-fucose from GDP-L-[14C]-fucose to oligosaccharides from human milk. An α-(1→4)-L-fucosyltransferase that synthesizes lacto-N-fucopentaose II and lacto-N-difucohexaose I from lacto-N-tetraose and lacto-N-fucopentaose I, respectively, was detected in saliva samples of Le(a-b+) secretors and Le(a + b-) non-secretors in which Lea substance was secreted. This enzyme activity was demonstrable neither in saliva samples of Le(a-b-) secretors nor non-secretors. An α-(1→2)-L-fucosyltransferase, that synthesizes lacto-N-fucopentaose I from lacto-N-tetraose, was detected in saliva samples from Le(a-b+) secretors which secreted H and Leb substances and from Le(a-b-) secretors which secreted only H substance. An α-(1→3)-L-fucosyltransferase was present in all saliva samples of different ABO and Lewis blood groups, irrespective of their ABH secretor status of the donors. The fucosyltransferases in saliva were activated by Mn++ or Mg++ ions, and were inhibited by ATP, GTP and EDTA. They had a broad pH optimun between pH 5.0 and 6.5.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 10 (1983), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A β-galactoside α1 → 2 fucosyltransferase (H-enzyme) from human group O plasma which provides H blood group specificity to erythrocyte membranes has been purified approximately 22,000-fold by chromatography on DEAE-Sepharose CL-6B, GDP-hexanolamine-Sepharose 4B and SP-Sephadex C-50. The molecular weight of the H-enzyme was estimated to be 150,000 by gel filtration. Human group O erythrocyte membranes which had lost their H blood group activity by the action of α1 → 2 fucosidase were fucosylated by the transferase, and restored the H activity. Radioactive L-fucose appeared to be incorporated into glycolipid blood group substances of erythrocyte membranes. The activity of the α1 → 2 fucosyltransferase from human plasma, stomach mucosa, erythrocyte membranes and porcine stomach mucosa were specifically inhibited by the rabbit antiserum immunized with the preparation of human plasma H-enzyme. The anti-plasma H-enzyme antiserum did not inhibit the activities of α1 → 3 N-acetygalactosaminyltransferase (A-enzyme), α1 → 3 galactosyltransferase (B-enzyme), and β-N-acetylglucosaminide α1 → 3 and α1 → 4 fucosyltransferases from human plasma and stomach mucosa.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Company
    Nature biotechnology 1 (1983), S. 181-188 
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] It is shown here how mass spectrometry (MS) can be used for on–line data acquisition in fermentation. MS was applied in this work to analyze gas and liquid phases. Gas phase analysis allows fast and accurate measurement of all gases of interest (O2, N2, CO2, Ar, He etc.). Liquid phase ...
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 2293-2317 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Baker's yeast, Saccharomyces cerevisiae, was investigated for the combined influence of dissolved oxygen and glucose concentration in continuous culture. A reactor was operated at a range of dilution rates (0.1, 0.2, 0.25, 0.27, and 3.0 h-1), above and below the critical value that separates the oxidative and fermentation regions. For each dilution rate (D), steady states were established at each of five to ten different dissolved oxygen concentrations (DO) in the range of 0.01-5 mg/L. The use of on-line mass spectrometry facilitated the measurement of gaseous and dissolved O2, CO2, and ethanol. Intracellular carbohydrate, protein, RNA, DNA, lipid, and cytochrome concentrations were measured. Cell size measurements were reduced to specific surface areas. Cytochrome content showed up to 100% variation during a 20-day period of adaptation at D = 0.2 h-1 to low DO. Eventually, the culture behaved the same at DO = 0.05 mg/L as it did initially at 3 mg/L. At D = 0.2, 0.25, and 0.27 h-1, the transition between oxidation and fermentation was characterized by a critical DO which decreased with decreasing D. The X-D curves were shifted such that the critical D value was reduced with decreasing DO. Specific oxygen update rates varied with DO according to the saturation kinetics. Specific cell surface areas increased with decreasing DO. Cytochrome content generally decreased with decreasing DO, and QO2 could be linearly related to the total cytochrome content, which exhibited a maximum at D = 0.27 h-1.
    Additional Material: 31 Ill.
    Type of Medium: Electronic Resource
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