These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Characteristics of beta-lactoglobulin binding to the all-trans-retinal moiety covalently immobilized on Celite.
    Author: Wang Q, Swaisgood HE.
    Journal: J Dairy Sci; 1993 Jul; 76(7):1895-901. PubMed ID: 8345126.
    Abstract:
    All-trans-retinal was covalently immobilized on Celite and investigated as a bioselective adsorption matrix for beta-lactoglobulin. Two types of Celite supports were compared, indicating the best performance with 100/120 mesh, type R648. The R648 matrix yielded a high concentration (9.2 mumol/ml) of the ligand when the derivative was produced, and the derivatized matrix exhibited the best retention of beta-lactoglobulin. Binding of beta-lactoglobulin to the immobilized trans-retinal matrix is biospecific, but the affinity is dependent on pH and ionic strength. alpha-Lactalbumin is not bound to this bioselective adsorbant, so its elution was not retarded or affected by pH or buffer concentration. Affinity for beta-lactoglobulin was optimal at pH 5.14; a dissociation constant of 2.7 microM was obtained in .1 M buffer solutions. At pH 7.0, the affinity decreased 44-fold, and, below pH 3.5, no binding occurred. The estimated loading capacity based on chromatographic data was approximately 14 g/L (.75 mumol/ml) of support.
    [Abstract] [Full Text] [Related] [New Search]