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Angel Justiz-Vaillant 2020. Preparation of a protein-LA conjugated to horseradish peroxidase by the periodate method.. protocols.io https://dx.doi.org/10.17504/protocols.io.bjkzkkx6Copy Citation Copied
URL: https://dx.doi.org/DOI:10.17504/protocols.io.bjkzkkx6
Authors: Angel Justiz-Vaillant
Group: University of the West Indies, [email protected]
Summary: Protein LA, a novel hybrid protein, structurally contains 4 of the Ig Fc-binding and 4 of the Ig Fab binding regions on SpA with 4 of kappa light chain-binding sites of protein L. It has a MW of 65 kDa. Protein LA combines the binding properties of the both SpL and SpA and in some cases, give higher binding affinity than either protein alone. The binding of an Ig to SpL does not interfere with binding of another Ig molecule to the SpA domains and vice versa. Protein LA has been shown to bind effectively to immunoglobulins and their fragments from many species of animals [1]. Reference1. Justiz-Vaillant AA, Akpaka PE, McFarlane-Anderson N, Smikle MF. Comparison of techniques of detecting immunoglobulin-binding protein reactivity to immunoglobulin produced by different avian and mammalian species.West Indian Med J. 2013;62(1):12-20.
Affiliations: University of the West Indies St. Augustine
Version: 1
Publication Date: 2020
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