Primary structure of a BiP homologue in Eimeria spp
| Autor: | Fiona M. Tomley, Paul Patrick James Dunn, Janene M. Bumstead |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Signal peptide
Recombinant Fusion Proteins Molecular Sequence Data Antigens Protozoan Eimeria Complementary DNA parasitic diseases Animals Humans Amino Acid Sequence Endoplasmic Reticulum Chaperone BiP Peptide sequence Heat-Shock Proteins Base Sequence Sequence Homology Amino Acid General Veterinary biology cDNA library Endoplasmic reticulum Protein primary structure General Medicine DNA Protozoan biology.organism_classification Molecular biology Infectious Diseases Biochemistry Eimeria maxima Insect Science Parasitology Carrier Proteins Immunoglobulin Heavy Chains Chickens Eimeria tenella Molecular Chaperones |
| Zdroj: | Parasitology Research. 82:566-568 |
| ISSN: | 1432-1955 0932-0113 |
| DOI: | 10.1007/s004360050163 |
| Popis: | cDNA clones for homologues of a molecular chaperone of the endoplasmic reticulum called the immunoglobulin heavy-chain binding protein (BiP) have been isolated from Eimeria maxima and E. tenella sporozoite cDNA libraries. The E. tenella cDNA clone is of full length and has a predicted N-terminal signal sequence of approximately 30 amino acids and a C-terminal tetrapeptide sequence (His-Asp-Glu-Leu) for retention in the lumen of the endoplasmic reticulum. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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