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
  • 1
    Electronic Resource
    Electronic Resource
    ‘The Linea masculina,’ a new secondary sex character in Salientia (1935)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 57 (1935), S. 131-145 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A hitherto unknown secondary sex character in male frogs consists of a series of connective tissue bands which extends the entire length of both layers of the Obliquus muscle, at both their dorsal and ventral borders. Extensions of the ventral bands may be carried inward toward the midline at certain of the inscriptiones tendinae. These bands are named the Lineae masculinae. They are clearly visible in specimens from which the skin has been removed, and are visible even through the skin in living specimens of certain species of Kaloula.Ninety-one genera and 553 species of the frogs and toads of the world were examined for the presence or absence of this structure. It is distinct in the common American and European ranids, such as Rana pipiens and Rana esculenta. It is entirely absent in many genera. When present it is found only in adult males, being absent in sexually immature males and females of all ages. Examination revealed no seasonal variations in males of Rana pipiens. This indicates that there is some correlation between the expression of this character and the sexual hormones. No function is assigned to the Linea masculina, although it is suggested that it may be associated in some way with voice production. A discussion of the taxonomic distribution of the character is included.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1050570108
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Electrochemical measurements with glucose oxidase immobilized in polyacrylamide gel: Constant current voltametry (1971)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 13 (1971), S. 629-639 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Constant current voltametry was shown to be a suitable method for evaluation of electrodes containing immobilized oxidative enzymes as catalysts. The half-cell potential for the oxdidation of D-glucose at constant pH was measured at a series of constant dc currents, using glucose oxidase immobilized in a polyacrylamide gel-platinum gauze matrix as catalyst. Over the range studied the potential versus current data were linear and could be extrapolated to give the open-circuit half-cell potential at zero current. The difference between the measured potential and the open-circuit potential at a constant current was indicative of the loss in useful voltage due to concentration gradients within or adjacent to the enzyme electrode assembly. The relationship between the open-circuit potential and the pH of the reaction mixture was linear with a slope of -0.056, in good agreement with the predicted slope of -0.061.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260130504
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Potentiometric method for subatrate analysis using immobilized NAD+-dependent oxidoreductase enzymes (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 1905-1915 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Two coenzyme-dependent oxidoreductases, glucose dehydrogenase and alcohol dehydrogenase, were immobilized in polyacrylamide gel over a platinum grid matrix and used as enzyme electrodes to measure their substrate concentrations in buffered aqueous solutions. The immobilized enzymes were used to oxidize their substrates in the presence of NAD+. Ferricyanide was used as the redox mediator and electroactive specific. The determinations of glucose and ethenol were utilized to demonstrate and evaluate the performance of the system. The described methodology should be readily applicable to the analysis of numerous other substrates of coenzyme-dependent oxidoreductases.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260211103
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Immobilization of tyrosinase within polyacrylamide gels (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 1405-1412 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The enzyme tyrosinase (E.G. 1.14.18.1) has been immobilized in a polyacrylamide gel and intermittently assayed for enzyme activity over a period of 19 days using phenol as the substrate. The results of these studies indicate that the immobilized enzyme could be incorporated into a system to detect phenol and related compounds that are found in industrial effluents and as surface water contaminants.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260181007
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Potentiometric quantitation of glycerol using immobilized glycerol dehydrogenase (1982)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 971-975 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Glycerol dehydrogenase was immobilized in polyacrylamide gel layered over a small platinum screen and used to catalyze the oxidation of glycerol. In the presence of NAD+ and potassium ferricyanide, the coupling reaction generated a measurable electrical potential which was found to be Nernstian with respect to the glycerol concentration range of 10-4M to 10-1M. The reproducibility of the measurement and the optimal conditions for glycerol determination were described.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260240416
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Electrochemical evaluation of glucose oxidase immobilized by different methodsPresented in part at the 7th intersociety energy conversion engineering conference, September 25-29, 1972, San Diego, California. (1975)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 17 (1975), S. 413-422 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Glucose oxidase electrodes were constructed on a platinum screen using polyacrylamide gel, glutaraldehyde crosslinking, and glutaraldehyde crosslinking with +0.04 volts dc on the platinum screen as the methods of enzyme immobilization. The electrodes were evaluated in an electrochemical cell for the oxidation of glucose at the enzyme electrode and the reduction of oxygen at a platinum auxiliary electrode, using constant current voltametry or under external load operation. The method of immobilization affected the extrapolated opencircuit potential as well as the half-cell potential and the steady current under external load operation. The charged glutaraldehyde electrode gave the best current performance; however, the small output (microamps) indicated that major problems in electron transfer from an enzyme catalyst to an external circuit must be resolved before such electrodes can be used in practical application.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260170309
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Immobilization of lactase on carbon (1975)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 17 (1975), S. 1695-1696 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260171111
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Immobilization of nitrate reductase within polyacrylamide gels (1976)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 18 (1976), S. 1643-1645 
    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.260181115
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    A miniature palladium-palladium-oxide enzyme electrode for urea determination (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 642-645 
    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: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260617
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Electrochemical evaluation of lactate dehydrogenase immobilized in polyacrylamide gels (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 1785-1792 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Lactate dehydrogenase (EC 1.1.1.27) has been immobilized in polyacrylamide gels over a platinum grid matrix. The immobilized enzyme is used to oxidize L-lactate in the presence of nicotinamide adenine dinucleotide (NAD+) and femcyanide. The NADH produced is then chemically oxidized back to NAD+by ferricyanide. The coupled reduction of ferricyanide ions to ferrocyanide ions results in a measurable electrochemical potential. This measurable zero-current potential is found to be Nernstian in nature and directly proportional to the logarithm values of L-Iactate concentration over the range of 2 × 10-5to 5 × 10-2M. The results indicate that immobilized lactate dehydrogenase can be incorporated into a system to detect L-Lactate acid in aqueous solutions.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260191205
    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...