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Subject: search.filters.subject.beta-lactoglobulin

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Now showing 1 - 9 of 9
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    Rational crystallization of beta -lactoglobulin and vitamin D-3 complex reveal a secondary binding site
    (2008-01-01)
    Chen, Chun-Jung
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    Guan, Hong-Hsiang
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    Yang, Ming-Chi
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    Moo, Simon J. T.
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    生物科技學系
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    A novel two-dimentional gel electrophoresis for studing the cress-linking between beta-Lactoglobulin and milk proteins
    (2005-01-01)
    Chen, W. L.
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    Huang, M. T.
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    Mao, S. J. T.
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    交大名義發表
    ;
    National Chiao Tung University
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    Distinction between dry and raw milk using monoclonal antibodies prepared against dry milk proteins
    (2004-08-01)
    Chen, WL
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    Huang, MT
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    Liu, HC
    ;
    Li, CW
    ;
    Mao, SJT
    It is well established that the heating process during the preparation of dry milk (DMLK) causes structural changes in some milk proteins. However, because such changes are subtle, whether they can be detected by an immunochemical approach remains questionable. The present study attempted to develop a sensitive mAb that might distinguish the DMLK from freshly prepared raw milk. To test this possibility, we immunized mice with commercially prepared DMLK and produced a panel of mAb. From 900 hybridomas screened using an ELISA, 4 clones were found to be specific to DMLK; the other 68 clones recognized both DMLK and raw milk. In contrast to polyclonal antibodies, only the specific mAb could detect the DMLK spiked into the raw milk at as low as 5% in concentration (vol/vol). Western blot analysis shows that these specific mAb were all directed against beta-lactoglobulin (LG) and LG-milk protein conjugates. These mAb reacted with raw milk heated at 95 for 15 min; the reaction with LG-conjugates, however, was abolished when treated with reducing reagent. Thus, results suggests that a new antigenic epitope was exposed in a heating process, and the thio group of LG cross linked with other protein moiety played a provocative role in mAb recognition. A hypothetical model with respect to the interaction between the mAb and DMLK is proposed and discussed.
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    Distinguish between native and thermally denatured 5-lactoglobulin using a monoclonal antibody as a probe.
    (2005)
    Mao, S. J. T.
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    Chen, W. L.
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    Yang, M. C.
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    Liu, W. T.
    ;
    交大名義發表
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    Distinguish between native and thermally denatured beta-lactoglobulin using a monoclonal antibody as a probe
    (2005)
    Mao, S. J. T.
    ;
    Chen, W. L.
    ;
    Yang, M. C.
    ;
    Liu, W. T.
    ;
    交大名義發表
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    Residues 69-74 of beta-lactoglobulin are responsible for a monoclonal antibody binding to thermal denatured lactoglobulin
    (2005)
    Song, C. Y.
    ;
    Yang, M. C.
    ;
    Mao, S. J. T.
    ;
    交大名義發表
    ;
    National Chiao Tung University
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    Residues 69-74 of beta-lactoglobulin are responsible for a monoclonal antibody binding to thermal denatured lactoglobulin.
    (2005)
    Song, C. Y.
    ;
    Yang, M. C.
    ;
    Mao, S. J. T.
    ;
    交大名義發表
    ;
    National Chiao Tung University
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    Antioxidant nature of bovine milk beta-lactoglobulin
    (2007-02-01)
    Liu, H. C.
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    Chen, W. L.
    ;
    Mao, S. J. T.
    ;
    生物科技學系
    ;
    Department of Biological Science and Technology
    Heating is necessary for processing milk in the dairy industry, which evidently produces a conformational change in beta-lactoglobulin (beta-LG). beta-Lactoglobulin, a major protein that accounts for approximately 10 to 15% of total milk proteins, is a globular protein consisting of 162 AA with a relative molecular mass of 18.4 kDa. The purpose of the present study was to determine the antioxidant role of beta-LG in milk and the possible mechanism involved. We showed that beta-LG is a mild antioxidant whose potency is less than that of vitamin E and probucol (the latter being an antioxidant used for clinical therapy). The conversion of the beta-LG monomer to dimer was responsible, in part, for the mode of action in protecting low- density lipoproteins against copper-induced oxidation. Cross-linking the free thiol groups of beta-LG by heating (100 degrees C for 2 min), or chemically modifying the beta-LG by carboxymethylation to block the thiol groups resulted in a substantial loss of antioxidant activity. The data suggest that Cys-121 plays an essential role in the antioxidant nature of beta-LG. By using an anti-LG antibody affinity column to deplete the beta-LG from milk, we observed from the lost antioxidant activity that beta-LG contributes approximately 50% of the total activity. Because beta-LG is extremely sensitive to thermal denaturation, to maintain its antioxidant nature, dairy products consumed daily should not be overheated in order to maintain its antioxidant nature.
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    Evidence for beta-lactoglobulin involvement in vitamin D transport in vivo- role of the gamma-turn (Leu-Pro-Met) of beta-lactoglobulin in vitamin D binding
    (2009-04-01)
    Yang, Ming Chi
    ;
    Chen, Nai Chi
    ;
    Chen, Chun-Jung
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    Wu, Chin Yun
    ;
    Mao, Simon J. T.
    beta-lactoglobulin (LG) is a major bovine milk protein, containing a central calyx and a second exosite beyond the calyx to bind vitamin D; however, the biological function of LG in transporting vitamin D remains elusive. Crystallographic findings from our previous study showed the exosite to be located at the pocket between the alpha-helix and beta-strand I. In the present study, using site-directed mutagenesis, we demonstrate that residues Leu143, Pro144 and Met145 in the gamma-turn loop play a crucial role in the binding. Further evidence is provided by the ability of vitamin D(3) to block the binding of a specific mAb in the gamma-turn loop. Using the mouse (n = 95) as an animal model, we initially demonstrated that LG is a major fraction of milk proteins responsible for uptake of vitamin D. Most interestingly, dosing mice with LG supplemented with vitamin D(3) revealed that native LG containing two binding sites gave a saturated concentration of plasma 25-hydroxyvitamin D at a dose ratio of 2 : 1 (vitamin D(3)/LG), whereas heated LG containing one exosite (lacking a central calyx) gave a ratio of 1 : 1. We have demonstrated for the first time that LG has a functional advantage in the transport of vitamin D, indicating that supplementing milk with vitamin D effectively enhances its uptake.