Primary structure of a BiP homologue in Eimeria spp.
Copyright policy )Primary structure of a BiP homologue in Eimeria spp.
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.
- Pirbright Institute United Kingdom
- Newbury College United States
Base Sequence, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Molecular Sequence Data, Antigens, Protozoan, DNA, Protozoan, Animals, Humans, Eimeria, Amino Acid Sequence, Carrier Proteins, Immunoglobulin Heavy Chains, Chickens, Endoplasmic Reticulum Chaperone BiP, Eimeria tenella, Heat-Shock Proteins, Molecular Chaperones
Base Sequence, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Molecular Sequence Data, Antigens, Protozoan, DNA, Protozoan, Animals, Humans, Eimeria, Amino Acid Sequence, Carrier Proteins, Immunoglobulin Heavy Chains, Chickens, Endoplasmic Reticulum Chaperone BiP, Eimeria tenella, Heat-Shock Proteins, Molecular Chaperones
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