Characterization of Human B Cell Proteins Binding Specifically to Uveitopathogenic Peptide 1169-1191 of Bovine IRBP
| Autor: | M.D. Desmet, B. Wiggert, K. Rengarajan, Gerald J. Chader |
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| Rok vydání: | 1994 |
| Předmět: |
Molecular Sequence Data
Biophysics Peptide Biology Human b cell Biochemistry Adenosine Triphosphate Lewis rats Animals Humans Amino Acid Sequence Eye Proteins Molecular Biology Actin chemistry.chemical_classification B-Lymphocytes Molecular mass Human patient Blood Proteins Cell Biology Molecular biology Peptide Fragments eye diseases Rats Retinol-Binding Proteins Interphotoreceptor retinoid-binding protein chemistry Rats Inbred Lew Cattle Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 204:799-806 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1994.2530 |
| Popis: | Peptide 1169-1191 is a major uveitopathogenic determinant of bovine Interphotoreceptor Retinoid Binding Protein (IRBP) in Lewis rats. Previously, we identified two proteins with approximate molecular masses of 72 and 74 kDa and one with a molecular mass of 40 kDa from B cells of naive Lewis rats and EBV-transformed B cells from a human patient with ocular Behcet′s disease that bind to bovine IRBP peptide 1169-1191. In this study, we have partially characterized these proteins. The two proteins with molecular masses 72 and 74 kDa belong to the HSP 70 family of proteins and the 40-kDa protein is actin. |
| Databáze: | OpenAIRE |
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