Jacalin-IgA interaction: existence of two binding sites?

The effect of bovine serum albumin (BSA) on jacalin-IgA interaction was investigated using two types of jacalin isolated from different batches of Malaysian jackfruit seeds. Our data demonstrated that BSA inhibits the lectin-immunoglobulin inteaction in both cases. 0.1 percent (w/v) of BSA demonstra...

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Bibliographic Details
Main Authors: Onn Haji Hashim, Ng, C.L., Mohd Iskandar Nik Jaafar (Malaya Univ., Kuala Lumpur (Malaysia). Dept. of Biochemistry)
Format: Proceedings Paper
Language:English
Published: Persatuan Biokimia Malaysia 2013
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Online Access:http://agris.upm.edu.my:8080/dspace/handle/0/4310
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Summary:The effect of bovine serum albumin (BSA) on jacalin-IgA interaction was investigated using two types of jacalin isolated from different batches of Malaysian jackfruit seeds. Our data demonstrated that BSA inhibits the lectin-immunoglobulin inteaction in both cases. 0.1 percent (w/v) of BSA demonstrated approximately 50 percent binding inhibition. Addition of BSA enhanced the inhibitory effect of D-Gal on the jacalin-IgA interaction. The data suggests that the binding of jacalin to IgA occurs at two distinctive sites.