1. An image recording device comprising:
a feed unit that feeds a recording medium,
a transport unit that, by rotating a first drive roller and a second drive roller across which a recording medium is stretched, transports the recording medium fed by the feed unit from the first drive roller to the second drive roller,
a support member that supports the recording medium between the first drive roller and the second drive roller,
a recording unit that ejects a liquid on the recording medium supported on the support member and records an image,
a detection unit that is disposed between the support member and the second drive roller to detect tension of the recording medium moving toward the second drive roller away from the support member,
a take up unit that takes up the recording medium from the second drive roller, and
a control unit that adjusts tension of the recording medium between the first drive roller and the second drive roller by controlling the torque of the second drive roller based on the tension of the recording medium detected by the detection unit.
2. An image recording device according to claim 1, wherein
the recording unit ejects as a liquid a photo curing ink that is cured by light, and
the image recording device according to claim 1 further comprises a light radiating unit that radiates light on the ink ejected from the recording unit onto the recording medium.
3. An image recording device according to claim 1, further comprising a driven roller that winds the recording medium toward the second drive roller away from the support member, wherein the detection unit is provided on the driven roller.
4. An image recording device according to claim 1, wherein the support member is a drum on which the recording medium is wound, and rotates by receiving a frictional force with the recording medium transported by the transport unit.
5. The image recording device according to claim 1, wherein
the control unit adjusts the tension of the recording medium by controlling the torque of the second drive roller without giving a difference in a circumferential velocity of the first drive roller and a circumferential velocity of the second roller.
6. An image recording method comprising:
feeding a recording medium;
supporting on a support member a recording medium transported from a first drive roller to a second drive roller by rotating the first drive roller and the second drive roller across which the recording medium is stretched;
ejecting liquid on the recording medium supported on the support member to record an image;
detecting by a detection unit disposed between the support member and the second drive roller tension of the recording medium moving toward the second drive roller away from the support member;
adjusting tension of the recording medium between the first drive roller and the second drive roller by controlling the torque of the second drive roller based on the tension detected by the detection unit; and
taking up the recording medium from the second drive roller.
7. The image recording method according to claim 6, wherein
adjusting the tension of the recording medium includes controlling the torque of the second drive roller without giving a difference in a circumferential velocity of the first drive roller and a circumferential velocity of the second roller.
The claims below are in addition to those above.
All refrences to claim(s) which appear below refer to the numbering after this setence.
What is claimed is:
1. A system comprising a solid surface, wherein the surface has attached thereto one or more MHC monomer or modified MHC monomer wherein the monomer denatures under denaturing conditions and reconstitutes to form a ternary complex containing a suitable MHC-binding peptide under reconstituting conditions.
2. The system of claim 1, wherein the solid surface is a bead.
3. The system of claim 1, wherein the solid surface is in a microtiter plate.
4. The system of claim 1, wherein the solid surface is suitable for screening in a high throughput system.
5. The system of claim 1, wherein attachment of the monomer to the solid surface is reversible.
6. The system of claim 1, wherein attachment of the monomer to the solid surface is cleavable.
7. The system of claim 1, wherein the solid surface is coated with a first binding ligand and the C-terminal end of the monomer is provided with a second binding ligand, wherein the first ligand binds specifically with the second ligand.
8. The system of claim 7, wherein the first binding ligand is selected from avidin, streptavidin, neutravidin, StrepTactin and monomeric avidin and the second binding ligand is biotin.
9. The system of claim 8, wherein the second binding ligand is attached to the monomer via a C-terminal end.
10. The system of claim 1, wherein the denaturing conditions comprise a pH of about 2 to about 4.
11. The system of claim 1, wherein the system further comprises an anti-MHC antibody that binds specifically to a conformational epitope that is present in the reconstituted monomer and absent in the denatured monomer.
12. The system of claim 1, wherein the reconstituting conditions include a pH of from about 7 to about 8.5.
13. The system of claim 1, wherein the system further comprises beta-2 microglobulin.
14. The system of claim 1, wherein the monomer is HLA class I.
15. The system of claim 14 further comprising an anti-MHC class I monoclonal antibody, wherein the monoclonal antibody specifically binds to a reconstituted monomer and does not bind to a denatured monomer.
16. The system of claim 15, wherein the monomer is HLA class I and the system further comprises beta-2 microglobulin and a suitable HLA-binding peptide of from about 8 to about 12 amino acids; wherein a reconstituted monomer binds to the beta-2 microglobulin and the suitable peptide under reconstituting conditions.
17. The system of claim 15, wherein the monoclonal antibody is produced by hybridoma B9.12.1
18. The system of claim 1 or 16, wherein the solid surface coated with the monomers is in a dried form.
19. A kit comprising the system of claim 1, 16 or 17.
20. The kit of claim 19 further comprising an instruction.
21. The kit of claim 20 further comprising a control peptide to which the MHC monomer binds in a reconstituted form.
22. A method for determining binding between a MHC monomer or modified MHC monomer and a putative MHC-binding peptide therefor, said method comprising:
incubating under reconstituting conditions a solid surface having attached thereto a plurality of MHC monomers or modified MHC monomers in the presence and absence of the putative MHC-binding peptide, wherein the monomers have been denatured and reconstitute to form a ternary complex containing a suitable MHC-binding peptide under reconstituting conditions, and
determining binding to the MHC monomers after contact therewith of a monoclonal antibody that binds to the ternary complex but does not bind to dissociated components of the complex, which binding of the antibody indicates binding of the monomers with the putative MHC-binding peptide.
23. The method of claim 22, wherein the denaturing conditions include a pH in the range from about 2 to about 4.
24. The method of claim 22, further comprising separately incubating the monomers with a standard MHC-binding peptide for the monomers under the reconstituting conditions in the presence of the monoclonal antibody, and wherein the determining includes comparing binding of the antibody caused by the standard peptide to the binding of the antibody caused by the putative MHC-binding peptide.
25. The method of claim 24, wherein the monomers are HLA class I, the monoclonal antibody is an anti-MHC-class I antibody, and the reconstituting conditions include the presence of sufficient beta-2 microglobulin for reconstitution of the monomers.
26. The method of claim 25, wherein the monomers are HLA subclass A, B or C.
27. The method of claim 22, wherein the monoclonal antibody is provided with a detectable label and the determining includes detecting the detectable label.
28. The method of claim 27, wherein the detectable label is a secondary antibody that specifically binds to the monoclonal antibody.
29. The method of claim 28, wherein the detectable label is fluorescent.
30. The method of claim 22, wherein the solid surface is the wells of a microtiter plate or beads and the determining includes reading fluorescence with a fluorimeter.
31. The method of claim 30, wherein the detecting further comprises detecting the fluorescence using high throughput scanning.
32. The method of claim 22, wherein the solid surface is coated with avidin and the monomers are biotinylated to attach to the solid surface.
33. The method of claim 22, wherein attachment of the monomers to the solid surface is reversible.
34. The method of claim 22, wherein attachment of the monomers to the solid surface is cleavable.
35. A method for determining the degree of binding affinity of an MHC monomer or modified MHC monomer for a putative MHC-binding peptide therefor, said method comprising:
incubating at least one denatured MHC monomer or modified MHC monomer attached to a solid surface with the putative MHC-binding peptide and a monoclonal antibody that specifically binds to a conformational epitope in a ternary complex containing a corresponding reconstituted MHC monomer and does not bind to any dissociated component of the ternary complex, wherein the incubation is under reconstituting conditions; and
comparing binding of the monoclonal antibody to a ternary complex that contains the putative MHC-binding peptide with binding of the monoclonal antibody to a corresponding ternary complex containing the monomer and a known MHC-binding peptide, wherein a difference in the bindings indicates the relative degree of binding affinity of the reconstituted monomer for the putative MHC-binding peptide.
36. The method of claim 35, wherein the reconstituting conditions include a temperature in the range from about 18 C. to about 37 C.
37. The method of claim 35, wherein the reconstituting conditions include a temperature in the range from about 4 C. to about 8 C.
38. The method of claim 35, wherein the reconstituting conditions include a pH in the range from about 7 to about 8.5.
39. The method of claim 35, wherein the reconstituting conditions include the presence of a suitable reconstitution buffer.
40. The method of claim 39, wherein the suitable reconstitution buffer comprises polyoxyethylene(20) sorbitan monolaurate.
41. The method of claim 35, wherein the incubating is for a period of from about 12 hours to about 48 hours.
42. The method of claim 35, wherein the antibody is provided with a detectable label and wherein the comparison of binding comprises detecting a difference in the respective signals produced by the detectable label resulting from binding of the antibody thereto.
43. The method of claim 42, wherein the antibody is labeled with a fluorescent label and the comparison of binding comprises detecting a difference in the respective fluorescence resulting from binding of the antibody thereto.
44. The method of claim 43, wherein the solid surface is the wells of a microtiter plate or beads and the detecting includes reading the fluorescence with a fluorimeter.
45. The method of claim 44, wherein the detecting further comprises detecting the fluorescence using a high throughput scanning.
46. The method of claim 35 wherein the fluorescent label is fluorescein isothiocyanate (FITC).
47. The method of claim 35, wherein the monomers are HLA class I and further bind with beta-2 microglobulin in reconstituting conditions and the monoclonal antibody is an anti-MHC-class I monoclonal antibody.
48. The method of claim 47, wherein the monomers are selected from HLA-A, HLA-B, and HLA-C.
49. The method of claim 47, wherein the monomers are chimeric.
50. The method of claim 35, wherein the monoclonal antibody is produced by hybridoma B9.12.1.
51. The method of claim 42, wherein the difference in the binding is compared after incubating the ternary complex containing the putative MHC binding peptide and the known peptide under conditions comprising a dissolution-testing temperature for a time sufficient to indicate the relative dissolution rate of the putative MHC-binding peptide.
52. The method of claim 51, wherein the dissolution-testing temperature is in the range from about 4 C. to about 37 C.
53. The method of claim 52, wherein the time is from about 2 hours to about 48 hours.
54. The method of claim 28, wherein the detectable label is peroxidase.