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    • Keywords


      Hyaluronan; hyaluronan binding protein; D-mannosylated albumin

    • Abstract


      We have earlier reported that overexpression of the gene encoding human hyaluronan-binding protein (HABP1) is functionally active, as it binds specifically with hyaluronan (HA). In this communication, we confirm the collapse of the filamentous and branched structure of HA by interaction with increasing concentrations of recombinant-HABP1 (rHABP1). HA is the reported ligand of rHABP1. Here, we show the affinity of rHABP1 towards D-mannosylated albumin (DMA) by overlay assay and purification using a DMA affinity column. Our data suggests that DMA is another ligand for HABP1. Furthermore, we have observed that DMA inhibits the binding of HA in a concentration-dependent manner, suggesting its multiligand affinity amongst carbohydrates. rHABP1 shows differential affinity towards HA and DMA which depends on pH and ionic strength. These data suggest that affinity of rHABP1 towards different ligands is regulated by the microenvironment.

    • Author Affiliations


      Rajeev Kumar1 Nirupam Roy Choudhury2 Dinakar M Salunke3 K Datta

      1. Biochemistry Laboratory, School of Environmental Sciences, Jawaharlal Nehru University, New Delhi - 110 067, India
      2. Genetic Engineering Unit, Jawaharlal Nehru University, New Delhi - 110 067, India
      3. National Institute of Immunology, Aruna AsafAli Marg, New Delhi - 110 067, India
    • Dates

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