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KMID : 0438619930170020093
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Journal of Oral Biology
1993 Volume.17 No. 2 p.93 ~ p.100
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Receptor Binding Characteristics of Macrophage Inflammatory Protein-α and -β
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Oh, Kwi-Ok
Jeong, Seung Ryong/Yu, Kang Ryeol/Oh, Hee Jeong/Lee, Dong Whan/Lee, Seong Hee/Kwak, Yak Hoon
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Abstract
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We purified the recombinant murine MIP-lα (rmMIP-1α) and rmMIP-1β, and used the proteins to determine receptor-bearing cells and the binding propenies and the relationship between MIP-lα and MIP-1β in the receptor binding properties.
Direct receptor binding analysis using radioiodinated rmMIP-lα or -1β indicated a single class of high affinity binding site with a Kd of approximately 0.9-1.5×10^(-() M and the presence of approximately 30-4000 binding sites per cell from cytolytic T cell, macrophage, myeloid strm cell, endothelial cell, helper T cell, bone marrow cell, splenocyte, and B cell.
Competition binding assays indicated MIP-lα and -1β were able to recognize the common binding site. This is in good agreement with the resutts from biological function test.
Results from cross-linking study and receptor blotting experiment demonstrated that binding molecule might be 30 KDa monomer or 60 KDa homodimer.
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