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. 1998 Sep 7;188(5):973–978. doi: 10.1084/jem.188.5.973

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Characteristics of sQa-1^b/β₂m secreted from transfected D. melanogaster cells and its specific binding to immobilized QdmC5 peptide. (A) After concentration and purification, the supernatant from Qa-1^b/β₂m-transfected Drosophila cells was resolved on a 15% SDS-PAGE, and stained using Coomassie brilliant blue. Arrows, Qa-1^b heavy chain (Hc) and β₂m. (B–D) SPR demonstrating binding of sQa-1^b/β₂m to immobilized QdmC5. Sensorgrams were obtained using injection volumes of 20 μl at a rate of 1 μl/min. Mass increase due to macromolecular binding is measured in resonance units (RU). Arrowheads, Start (↑ ) and end (↓ ) of the injection. (B) Injection of 0.5 μM sQa-1^b or sM3. (C) 0.5 μM sQa-1^b was run over the chip alone, or in the presence of 20 μM Qdm (AMAPRTLLL), QdmC5 (AMAPCTLLL), or two control peptides, PMLTMCHAL and YPHFMPTNL. (D) 0.5 μM sQa-1^b was run at 1 μl/min for 20 min over immobilized QdmC5 in the absence or presence of competitor peptides. Results are presented as relative binding of sQa-1^b, where 0 represents binding in the presence of 20 μM Qdm (25 RU), and 1 is the binding in the absence of peptide (263 RU). *, +, and O represent binding in the presence of 20 μM of the entire 24-mer D^d leader, MGAMAPRTL and MAPRTLLLL, respectively.

Characteristics of sQa-1^b/β₂m secreted from transfected D. melanogaster cells and its specific binding to immobilized QdmC5 peptide. (A) After concentration and purification, the supernatant from Qa-1^b/β₂m-transfected Drosophila cells was resolved on a 15% SDS-PAGE, and stained using Coomassie brilliant blue. Arrows, Qa-1^b heavy chain (Hc) and β₂m. (B–D) SPR demonstrating binding of sQa-1^b/β₂m to immobilized QdmC5. Sensorgrams were obtained using injection volumes of 20 μl at a rate of 1 μl/min. Mass increase due to macromolecular binding is measured in resonance units (RU). Arrowheads, Start (↑ ) and end (↓ ) of the injection. (B) Injection of 0.5 μM sQa-1^b or sM3. (C) 0.5 μM sQa-1^b was run over the chip alone, or in the presence of 20 μM Qdm (AMAPRTLLL), QdmC5 (AMAPCTLLL), or two control peptides, PMLTMCHAL and YPHFMPTNL. (D) 0.5 μM sQa-1^b was run at 1 μl/min for 20 min over immobilized QdmC5 in the absence or presence of competitor peptides. Results are presented as relative binding of sQa-1^b, where 0 represents binding in the presence of 20 μM Qdm (25 RU), and 1 is the binding in the absence of peptide (263 RU). *, +, and O represent binding in the presence of 20 μM of the entire 24-mer D^d leader, MGAMAPRTL and MAPRTLLLL, respectively.