| Title: | Molecular and structural properties of three autoimmune IgG monoclonal antibodies to histone H2B. |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1016117 |
| landingPage: |
http://www.iedb.org/assay/1691686 |
| type: |
Literature
|
| publicationVenue: |
J Biol Chem
|
| dates: |
2000
|
| study type: | b cell assays |
| subject species: | Bos taurus |
| fullName: |
M Monestier
P Decker
J P Briand
J L Gabriel
S Muller
|
| method: |
antigen inhibition
|
| name: |
Molecular and structural properties of three autoimmune IgG monoclonal antibodies to histone H2B.
|
| description: |
The epitope competed with a longer peptide of residues 1-25 in ELISA. The binding of PR1–1 is totally abolished when P1 is substituted with A1 and moderately affected when K11 is replaced with an alanine residue. LG2–2 reactivity is abolished by the P1 to A1 substitution and only moderately affected by the K11 to A11 replacement. In contrast with PR1–1, LG2–2 binding is only partially decreased by the K5 to A5 replacement. The LG2-2 mAb was of the IgG2aκ subtype.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |