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  • Biochemistry and Biotechnology  (3)
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  • 1
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Conditions for the preparation of microcapsules containing asparaginase by interfacial polymerization were investigated.The activity of microcapsules prepared under the optimal conditions was about 37% compared with that of native asparaginase. Particle size of microcapsules could be controlled by determining the stirring rate and concentration of Span 85. The membranes of microcapsules were resistant to mechanical shock or attack of chymotrypsin, and no leakage of asparaginase from microcapsules was observed.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Various methods were tried for the immobilization of aspartase, and the preparation having the highest activity was obtained when partially purified aspartase from Escherichia coli was entrapped into polyacrylamide gel Iattice. Enzymatic properties of the immobilized aspartase were investigated and compared with those of the native aspartase. With regard to optimum pH, temperature, concentration of Mn++, kinetic constants and heat stability, no marked difference was observed between the native and immobilized aspartases.By employing an enzyme column packed with the immobilized aspartase, conditions for continuous production of L-aspartic acid from ammonium fumarate were investigated. When a solution of 1M ammonium fumarate (pH 8.5, containing 1mM MnCl2) was passed through the aspartase column at the flow rate of SV = 0.08 at 37°C, the highest rate of reaction was attained. From the column effluents, L-aspartic acid was obtained in a good yield.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Proteins in the cytosol, post-nuclear particulate and nuclear fractions from dorsolateral and ventral prostates of rats were analyzed and compared by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Protein species separated in the gel were stained with Coomassie Brilliant Blue R-250 (CBB), and expressed as (apparent molecular weight of the respective species x 10-3)K. (i) In the cytosol fraction the contents of 30K, 67K, 110K, and 120K proteins were abundant in the dorsolateral prostate. On the other hand, 14K and 16K proteins were specific to the ventral prostate. By carbohydrate staining, major glycoproteins were found to be 120K and 16K for the dorsolateral and ventral prostates, respectively. (ii) In post-nuclear particulate fractions in both lobes, proteins having molecular weights greater than 42 000 were abundant. Of these, the contens of 65K, 105K and 120K were higher in the dorsolateral prostate than in the ventral prostate. Glycoproteins having the same apparent molecular weight as detected in the cytosol fractions were also found in the post-nuclear particulate fractions of both lobes. (iii) In the nuclear fraction H2A, H2B, H3 and H4 histones were fundamentally similar between the two lobes, whereas H1 histones including two subspecies were slightly but significantly higher in the ventral prostate than the dorsolateral prostate. The most remarkable difference between the lobes was the content of 20K in the dorsolateral prostate which was at least 20 times higher than that found in the ventral prostate.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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