ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Chemistry  (49)
  • Humans  (8)
  • Life and Medical Sciences
  • Space Transportation and Safety
  • 2005-2009  (10)
  • 1980-1984  (38)
  • 1970-1974  (15)
  • 1
    Electronic Resource
    Electronic Resource
    PPP calculations of the circular dichroism spectra of some dinucleoside phosphates (1972)
    New York : Wiley-Blackwell
    Biopolymers 11 (1972), S. 1091-1102 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Circular dichriosm (CD) spectra have been calculated for serveral dinucleoside phosphates using a variant of the Pariser-Parr-Pople π-electron molecular orbital method. This method does not require the prior knowledge of the experimental absorption spectra of transition moments of the bases forming the dinucleoside phosphates. Calculated spectra were obtained in good agreement with experimental spectra for four dinucleoside phosphates, ApA, UpU, GpA, and UpA, and reasonable agreement was obtained for ApG and ApU. The effect of changing conformation on the CD spectrum was studied for ApA, UpU, UpA, and ApU; the spectra of UpU, UpA, and ApU were sensitive to small change in conformation, whereas ApA was insensitive over the range of conformation studied. Further studies await detailed knowledge of the structure of dinucleoside phosphates in solution.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1972.360110511
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Synthesis and free radical ring-opening polymerization of 2-methylene-4-phenyl-1,3-dioxolaneThis research was supported in part by Grant No. DMR-77-28322 from the Polymer Program of the National Science Foundation. (1982)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 183 (1982), S. 1913-1920 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The cyclic ketene acetal, 2-methylene-4-phenyl-1,3-dioxolane (3), was shown to undergo free radical ring-opening polymerization to produce the polyester, poly[γ-(β-phenyl)butyrolactone]. The monomer 3 was synthesized by an acetal exchange reaction of chloroacetaldehyde dimethyl acetal with styrene glycol in an 87% yield followed by dehydrochlorination of the resulting cis and trans-2-chloromethyl-4-phenyl-1,3-dioxolane (2) with potassium tert-butoxide in tert-butyl alcohol in a 70% yield. 3 was shown to undergo essentially quantitative free radical ring-opening at all temperatures from 60-150°C and also nearly complete regioselective ring-opening with cleavage to give the more highly stable secondary benzyl free radical. Even in free radical copolymerization with styrene, methyl methacrylate, vinyl acetate, or 4-vinylpyridine, 3 gives essentially complete ring opening to introduce an ester groups into the backbone of the addition copolymer. The structures of the polymers were established by elemental analysis and 1H and 13C NMR spectroscopy.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1982.021830811
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Aspects of the ultrastructure of the alimentary canal and respiratory ducts in Xenopus laevis larvae (1972)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 138 (1972), S. 387-405 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The pharynx, intestine and respiratory duct of Xenopus laevis were examined by light and electron microscopy, at different stages of the metamorphic cycle, through climax.It is well known that preclimactic larvae are suspension feeders and that after climax specimens feed on solid food. It is shown that the histology of the pharynx and the alimentary canal changes in adaptation to the change in the mode of feeding.Suspension feeding utilises ciliary activity but after climax cilia have disappeared from the pharynx and alimentary canal, when new neuromuscular mechanisms are utilised in feeding.Other morpho-histological changes in various intestinal and respiratory tissues are likewise considered in terms of functional activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051380402
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Steady state multiplicity and stability of enzymatic reaction systems (1973)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 15 (1973), S. 1131-1145 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Several techniques for investigating the multiplicity and stability of open isothermal enzymatic reactors are discussed and some of the pitfalls in previous thinking pointed out. The example which is used to illustrate these methods exhibits several interesting features. Among these is the existence of a stable oscillatory state which surrounds a unique steady state which is asymptotically stable to certain finite disturbances.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260150611
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Analysis of fermentation processes using flow microfluorometry: Amylase and protease activities in Bacillis subtilis batch cultures (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 1657-1669 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Flow microfluorometry, which provides detailed information on the state of a microbial population, has been employed to characterize the Bacillus subtilis population during time intervals in which significant changes in the culture amylase activity occur. Four different batch experiments have been conducted, and the influences of inoculum age, fermentation temperature, and aeration rate on microbial population dynamics and amylase activity have been examined. Relatively high rates of amylase activity increase are observed twice during the batch, first as double cells initiate sporulation and later during germination. Rapid decreases in amylase activity are observed in highly (25-50%) sporulated populations, and in at least one experiment, during a transition from large, rounded protoplast forms to normal rod morphology. Amylase and protease activities do not follow parallel nor proportional trajectories in these 72 hr batch fermentations.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220809
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Plasmid stability in budding yeast populations: Steady-state growth with selection pressure (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 528-536 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Plasmid gene product accumulation in a cell population depends on the fraction of plasmid-containing cells and the distribution of single-cell plasmid content. These important population properties have been related to plasmid replication regulation and kinetics and to plasmid segregation rules at the single-cell level using population balance mathematical models. Budding yeast populations are considered in detail because of the practical potential of yeast host-vector systems and because of the model complications introduced by the asymmetric division pattern observed for Saccharomyces cerevisiae at all but the largest growth rates. Solutions are presented for several different reasonable models of plasmid replication and segregation. The results offer potential for identification of important qualitative features of yeast plasmid replication and of model parameter values from average and segregated experimental data on yeast populations.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260519
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Plasmid stability in budding yeast populations: Dynamics following a shift to nonselective medium (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 814-819 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260732
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes in porous supports: Effects of support-enzyme solution contacting (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 892-900 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Proteins have been immobilized in porous support particles held in a fixed-bed reactor through which protein solution is continuously circulated. Changing the recirculation flow rate alters the observed immobilization kinetics and the maximum enzyme loading which can be achieved for glucose oxidase and glucoamylase on carbodiimide-treated activated carbon and for glucoamylase immobilized on CNBr-Sepharose 4B. Direct microscopic examination of FITC-labelled protein in sectioned Sepharose particles and indirect activity-loading studies with activated carbon-enzyme conjugates all indicate that immobilized enzyme is increasingly localized near the outer surface of the support particles at larger recirculation flow rates. Restricted diffusion of enzymes may be implicated in this phenomenon. These contacting effects may be significant considerations in the scaleup of processes for protein impregnation in porous supports, since apparent activity and stability of the final preparation depend on internal protein distribution.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260812
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Genetically structured models forlac promoter-operator function in the Escherichia coli chromosome and in multicopy plasmids: Lac operator function (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 1372-1382 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A mathematical model based on known molecular interactions has been formulated to describe quantitatively regulation of expression of the lactose (lac) operon in the Escherichia coli chromosome and in multicopy plasmids. This model is genetically structured such that a nucleotide sequence change affecting transcription initiation at the lac promoter-operator influences one or very few directly corresponding model parameters. The model simulates chromosomal lac operon function in good agreement with previous experimental measurements for many lacl and lacO mutant systems as well as for diploid cells which carry F'lac episomes. Simulation results clearly show the loss of cloned lac operator regulation as the plasmid copy number increases, in agreement with experimental trends. The importance of this class of models in designing DNAs, organisms, and reactors for precise regulation of cloned gene expression is discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260261115
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Immobilized enzyme catalysis with reaction-generated pH change (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1345-1357 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Many enzyme-catalyzed reactions involve the liberation or consumption of hydrogen ions. In this paper a mathematical model is employed to investigate how such reactions behave when the enzyme is immobilized. Shifted pH optima, disappearance of an optimum pH, insensitivity to bulk pH, and very large effectiveness factors are some of the phenomena which appear as a result of pH coupling between the reaction and the enzyme's activity. Several of the qualitative features revealed by the model are consistent with earlier experimental observations. In addition, preliminary guidelines for optimal choice of enzyme support are suggested.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260161004
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...