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  • Biochemistry and Biotechnology  (5)
  • Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
  • 1980-1984  (7)
Document type
Keywords
Publisher
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Kinetics of enzymatic starch liquefaction: Simulation of the high-molecular-weight product distribution (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 1475-1484 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Enzymatic corn starch liquefaction with α-amylase was carried out. Molecular weight distributions of the resulting hydrolysates are presented using aqueous size exclusion chromatographic techniques. It is demonstrated that despite the fact that the enzyme employed reacts in a random endoacting manner, the product distributions are nonrandom. The results are explained in part by a multimerization process whereby the polymeric substrate molecules preferentially associate, forming intermolecular aggregates. These aggregates are either a consequence of the manner in which the material is deposited into the native granular structure of starch or due to intrinsic physical chemical properties of the polysaccharide. In the latter case, the results are shown to correspond to known multimerized amylose, although complete characterization of the polysaccharide is currently not available. The results presented are used to develop a simplified kinetic model of starch liquefaction and shown to simulate the product distributions accurately.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260261212
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The immunodetection of brain proteins blotted onto nitrocellulose from fixed and stained two-dimensional polyacrylamide gels (1984)
    Weinheim : Wiley-Blackwell
    Electrophoresis 5 (1984), S. 35-42 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Proteins visualised by Coomassie Blue staining of two-dimensional polyacrylamide gels of complex mixtures of brain proteins were blotted onto nitrocellulose sheets. The Coomassie Blue stain was transferred simultaneously and bound strongly to the nitrocellulose, giving a copy of the original gel pattern. Using specific antisera and a second antibody coupled to horseradish peroxidase, proteins in the original mixture could be detected on the nitrocellulose in quantities less than 25 ng. The Coomassie Blue and horseradish peroxidase stains were distinguishable by a suitable filter, allowing precise correlation of spots stained by Coomassie Blue with spots stained with the brown immunoperoxidase reaction product. The technique was used to identify related proteins in electrophoretograms of brain extracts from different animals.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150050107
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  • 3
    Electronic Resource
    Electronic Resource
    Improvements of isoelectric focusing in agarose for direct tissue isoelectric focusing (1982)
    Weinheim : Wiley-Blackwell
    Electrophoresis 3 (1982), S. 307-314 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Improvements of isoelectric focusing (IEF) in agarose are described that result in consistently obtaining broad, linear pH gradients in the range pH 4 to 9.2 at equilibrium. Cathodic drift has been reduced by the use of a blend of commercial carrier ampholytes and by incorporating lysine and arginine in the catholyte as spacers. Resolution has also been enhanced by the use of thin gels, supplemented with sorbitol and glycerol. In addition, a comparison of two agarose preparations for isoelectric focusing was performed using two commercial carrier ampholytes. To minimise background staining, Triton complexes were removed by modification of the fixing and clearing procedures. These modifications to IEF in agarose are being applied to direct tissue isoelectric focusing (DTIF) of normal and diseased human skeletal muscle.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150030602
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  • 4
    Electronic Resource
    Electronic Resource
    A novel human kidney-specific protein detected by two-dimensional electrophoresis: Isolation, radioimmunoassay, and immunohistochemical localization (1984)
    Weinheim : Wiley-Blackwell
    Electrophoresis 5 (1984), S. 362-369 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: High resolution two-dimensional polyacrylamide gel electrophoresis has been used to detect a soluble protein in extracts of human kidney which was not present in the electrophoretograms of other human tissues. This protein, coded kidney-acidic protein-60 (KAP-60) was purified to homogeneity and was characterized as having a native molecular weight of 85000, a monomer molecular weight of 35 000 and an isoelectric point of 5.6. KAP-60 was devoid of detectable carbohydrate or phosphate groups. Injection of the protein into rabbits produced antisera which were used to develop a radioimmunoassay for the protein and to localize the protein to specific cells within the kidney by the immunoperoxidase technique. A survey of human tissues by radioimmunoassay showed that KAP-60 was present in human kidney at approximately 150 times the concentration found in human liver and 300 times the level found in other human organs examined. Immunohistochemistry localized the protein to the proximal and collecting tubules in the kidney with no staining of glomeruli or distal tubules. The present study illustrates the use of high-resolution two-dimensional electrophoretic techniques in the detection of human tissue-specific proteins which may prove of clinical value in the biochemical diagnosis of tissue-specific damage.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150050608
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  • 5
    Electronic Resource
    Electronic Resource
    The application of direct tissue isoelectric focusing to the study of human skeletal muscle (1981)
    Weinheim : Wiley-Blackwell
    Electrophoresis 2 (1981), S. 251-258 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A method of direct tissue isoelectric focusing (DTIF) in agarose of human skeletal muscle is described. This particular method was developed to utilize the small amounts of tissue obtained by needle muscle biopsies performed for diagnostic purposes. 20 μm thick cryostat sections were adhered to the hydrophilic surfaces of small GelBond rectangles. These were then applied directly to the surface of the gels. A charge-balanced purified agarose was used to make the gels, which contained Triton X-100 to enhance protein solubilization. Stabilization of the pH gradient was attempted by employing a 3% w/v ampholyte which was a blend of 0.85% w/v pH 8-10.4 and 2.15 % w/v pH 3-10 Pharmalyte, by using anolyte regulation with 0.1 M aspartic acid and by focusing the gels under a CO2-extracted nitrogen atmosphere. Equilibrium of proteins stained by Coomassie Brilliant Blue R-250 was apparent as monitored by comigration of sections from both anode and cathode. With the exception of the cathode end, excellent resolution and reproducibility was achieved. Better cathode resolution was noted with non-equilibirium conditions. Preliminary zymograms of lactic dehydrogenase (LDH), using a tetrazolium technique, have shown consistent patterns of multiple isoenzymes, the basic components of which were best seen using non-equlibirium conditions.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150020410
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  • 6
    Electronic Resource
    Electronic Resource
    Comparison of sterols of pollens, honeybee workers, and prepupae from field sites (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 1 (1983), S. 25-31 
    Details
    ISSN: 0739-4462
    Keywords: honeybees ; pollens ; sterols ; field sites ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Sterols from pollen collected by foraging honeybees, Apis mellifera L, at seven field sites were compared with the sterols of foraging adults and/or prepupae collected from colonies at each site. Invariably, the composition of prepupal sterols was comparable to that found in previous cage studies using chemically defined diets containing various dietary sterols: 24-methyl-enecholesterol was the major sterol; sitosterol and isofucosterol were present in lesser, but significant amounts; and a trace amount of cholesterol was identified in each sample. This occurred even though some of the pollen sterols contained little 24-methylenecholesterol, sitosterol, or isofucosterol and a preponderance of certain other sterols, such as δ7-stigmasten-3β-ol and δ7,24(28)-campestadien-3β-ol in goldenrod and corn pollens, respectively. Thus the selective transfer and utilization of sterols in honeybees that have been demonstrated in cage studies with artificial diets were also shown to occur under field conditions.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940010104
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  • 7
    Electronic Resource
    Electronic Resource
    Identification of 20-hydroxyecdysone and ecdysone from the pupa of the gypsy moth, Lymantria dispar (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 1 (1984), S. 323-330 
    Details
    ISSN: 0739-4462
    Keywords: gypsy moth ; pupal ecdysteroids ; high-pressure liquid chromatography ; radioimmunoassay ; mass spectrometry ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Normal and reverse-phase high-performance liquid chromatography in conjunction with radioimmunoassay and mass spectrometry were used to identify the free and conjugated ecdysteroids (after enzymatic hydrolysis) from day-4 pupae of the gypsy moth, Lymantria dispar L. Seven ecdysteroids were searched for, but only 20-hydroxyecdysone (964 ng/g fresh weight) and ecdysone (367 ng/g fresh weight) were detected. Analysis of conjugated ecdysteriods after liberation by hydrolysis also indicated the presence of 20-hydroxyecdysone (21.6 ng/g fresh weight) and ecdysone (2.4 ng/g fresh weight). Neither 26-hydroxyecdysone nor the 3α-epimers of 20-hydroxyecdysone or ecdysone were detected.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940010404
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