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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Main Authors: | , , |
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Format: | Proceedings Paper |
Language: | English |
Published: |
Persatuan Biokimia Malaysia
2013
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Subjects: | |
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. |
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