| Autor: |
Yamamoto, Kazuo, Maruyama, Ichiro N., Osawa, Toshiaki |
| Předmět: |
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| Zdroj: |
Journal of Biochemistry; 2000, Vol. 127 Issue 1, p137-142, 6p |
| Abstrakt: |
Bauhinia purpurea lectin (BPA) is one of the β-galactose-binding leguminous lectins. Leguminous lectins contain a long metal-binding loop, part of which determines their carbohydrate-binding specificities. Random mutations were introduced into a portion of the cDNA coding BPA that corresponds to the carbohydrate-binding loop of the lectin. An library of the mutant lectin expressed on the surface of lambda foo phages was screened by the panning method. Several phage clones with an affinity for mannose or N-acetylglucosamine were isolated. These results indicate the possibility of making artificial lectins (so-called “cyborg lectins”) with distinct and desired carbohydrate-binding specificities. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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