Possible Mechanism for the Inhibition of Lectin-Erythrocyte Interaction in Presence of Endogenous Lectin Receptor
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Possible Mechanism for the Inhibition of
Lectin-Erythrocyte Interaction in Presence of
Endogenous Lectin Receptor
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| Creator |
Basu, Prabnab S
Datta, Pradip K Datta, Tapash K |
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| Subject |
Chemistry
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| Description |
The presence of hydrophobic sites in the lectin-I molecule was indicated by hydrophobic probes like
1-anilinonapthalene-8-sulfonic acid (ANS), 2-p-toluidinyl napthalene-6-sulfonic acid (TNS), N-phenyl-
1-napthylamine (NA) and rose bengal (RB). This was further confirmed by amino acid modifications
in the hydrophobic region of the lectin-I molecule. The binding of ANS, TNS, NA and RB to lectin-I
was affected in the presence of NaC1. The involvement of hydrophobic interactions in rice-bean
lectin-I-endogenous lectin receptor (ELR) complex were indicated by alterations in the circular
dichroism and fluorescence emission spectra. The percentage of/3-conformation (55-63%) of lectin-I
was decreased by addition of ELR. ELR on reacting with lectin-I reduced the fluorescence emissions
of the hydrophobic probes while fluorescence emission of ANS, TNS, NA and RB were greatly
enhanced in presence of lectin-I alone. N-aceyl-galactosamine did not change the fluorescence
emissions of any of the hydrophobic probes in presence or in absence of lectin-I. This demonstrates
that carbohydrate and hydrophobic sites may be different and non-interacting. It is proposed that the
ELR in reacting with lectin-I, induced conformational changes in the lectin-I molecule and thereby
affected its erythroagglutinating activity with human blood group "A" erythrocytes.
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| Date |
1996
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/703/1/BIOSCIENCE_REPORTS%2C_16_(6_)%2C_453%2D458[5].pdf
Basu, Prabnab S and Datta, Pradip K and Datta, Tapash K (1996) Possible Mechanism for the Inhibition of Lectin-Erythrocyte Interaction in Presence of Endogenous Lectin Receptor. Bioscience Reports, 16 (6). pp. 453-458. |
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| Relation |
http://dx.doi.org/10.1007/BF01198460
http://www.eprints.iicb.res.in/703/ |
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