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  • 1
    Electronic Resource
    Electronic Resource
    Single-cell protein from methanol with Enterobacter aerogenes (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 355-357 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An identifiedEnterobacter aerogenesutilizing methanol as a sole carbon source was studied for the optimization of biomass production and the reduction of its nucleic acid content. Results indicated that the highest yield and conversion were obtained at 0.5% methanol. The addition of seawater as a source of trace elements has an adverse effect. However, the addition of urea as source of nitrogen enhanced the growth of E. aerogenes. Heat shock at 60°C for 1 min followed by incubation at 50°C for 2 h caused 72.6% reduction in the nucleic acid.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260290310
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  • 2
    Electronic Resource
    Electronic Resource
    Selection of salt hydrate pairs for use in water control in enzyme catalysis in organic solvents (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 55 (1997), S. 367-374 
    Details
    ISSN: 0006-3592
    Keywords: salt hydrates ; water activity ; subtilisin ; lipase ; organic solvents ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The water activities (aw) of 13 salt hydrate pairs were determined from vapor pressure measurements; aw values for a subset were also estimated from a study of water transfer to isopropylether. The application of salt hydrates as water buffers was investigated in two models: (i) effect of hydration on the initial rate of subtilisincatalyzed transesterification of the nitrophenol ester of CBZ-alanine with butanol; and (ii) effect of hydrates on the equilibrium concentrations of reactants in the esterification of dodecanol and decanoic acid, catalyzed by lipase. Transfer of ions from salt to enzyme particles was also demonstrated. The implications of the results for the successful use of salt hydrates as water buffers are discussed. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 55: 367-374, 1997.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    A rapid screening technique for identifying murine monoclonal antibodies to human apolipoprotein A-I isoforms by Western blot analysis (1987)
    Weinheim : Wiley-Blackwell
    Electrophoresis 8 (1987), S. 552-556 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A rapid method for determining the reactivity of murine monoclonal antibodies with apolipoprotein A-I (Apo A-I) isoforms has been developed. The method consists of a rapid (1-2 h) prescreening of fusion well culture fluids by using an automated immunofluorescent assay (IF A) to identify fusion well cultures producing monoclonal antibody against Apo A-I and high-density lipoprotein (HDL). Immediately following the IFA procedure, immunodetection of the reactivity pattern of selected fusion well culture fluids is determined by using transblotted isoforms of Apo A-I previously separated by isoelectric focusing. Strips are prepared and stored at 4 °C in protein containing blocking solution before use. Preselected culture fluids could be tested within 6 h for qualitative reactivity with Apo A-I isoforms. Using this procedure we selected several monoclonal antibody-producing cultures for further studies on HDL metabolism based on their differing reactivities with Apo A-I isoforms. This technique should be easily transferable to other laboratories for assessing proteins having multiple isoforms since the crucial steps of separation and blotting can be optimized and performed before actual testing for antibody reactivity.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150081203
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  • 4
    Electronic Resource
    Electronic Resource
    Two-dimensional protein electrophoresis and multiple hypothesis testing to detect potential serum protein biomarkers in children with fetal alcohol syndrome (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1176-1183 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Image analysis ; Fetal alcohol syndrome ; Human serum proteins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Fetal alcohol syndrome (FAS) surveillance and intervention efforts are hampered by the lack of a specific biochemical test for diagnosis of the syndrome. Based on the hypothesis that abnormalities in growth and development (key features of FAS) involve altered protein metabolism, we analyzed serum proteins by two-dimensional gel electrophoresis and image analysis to search for potential protein biomarkers of FAS. Serum samples from 12 participants in whom FAS had been diagnosed and 8 sex- and age-matched participants whose mothers did not consume alcohol were analyzed in duplicate to determine whether the integrated intensities of matched proteins are significantly altered in children with FAS. Multiple hypothesis testing on 34 of the gels consisting of more than 1700 spots per gel revealed 21 proteins that we classified as potential protein biomarkers of FAS on the basis of significant t-test differences at p 〈 0.02. We classified 8 of the proteins as candidate biomarkers on the basis of significant concentration differences between case and control subjects at p 〈 0.01. One of the proteins is clearly an isoform of retinol binding protein; two appear in the area of the gel where alcohol dehydrogenase is expected to appear; one appears to be an isoform of alpha-1-antitrypsin; three appear to be isoforms of the beta-chain of haptoglobin; three may be forms of immunoglobulin light chains; and several others have not been associated with known proteins. No single protein differentiated all case subjects from control subjects, but stepwise canonical discriminant analyses revealed four groups of spots that distinguished between FAS case and control subjects with no misclassifications. Because of the small number of samples analyzed, we have not positively identified the proteins. It will be necessary to confirm our observations using additional samples before identifying each protein.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601195
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