Kinetics and the Mechanism of Interaction of the Endoplasmic Reticulum Chaperone, Calreticulin, with Monoglucosylated (Glc1Man9GlcNAc2) Substrate

Calreticulin is a lectin-like molecular chaperone of the endoplasmic reticulum in eukaryotes. Its interaction withN-glycosylated polypeptides is mediated by the glycan, Glc1Man9GlcNAc2, present on the target glycoproteins. In this work, binding of monoglucosyl IgG (chicken) substrate to calreticulin...

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Veröffentlicht in:	The Journal of biological chemistry 2000-08, Vol.275 (32), p.24348-24356
Hauptverfasser:	Patil, Anita R., Thomas, Celestine J., Surolia, Avadhesha
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - isolation & purification Calcium-Binding Proteins - metabolism Calreticulin Carbohydrate Sequence Cattle Chickens Endoplasmic Reticulum - metabolism Glycosylation Immunoglobulin G - chemistry Immunoglobulin Heavy Chains - chemistry Immunoglobulin Light Chains - chemistry Kinetics Microsomes, Liver - metabolism Molecular Chaperones - chemistry Molecular Chaperones - metabolism Molecular Sequence Data Oligosaccharides - chemistry Oligosaccharides - metabolism Ribonucleoproteins - chemistry Ribonucleoproteins - isolation & purification Ribonucleoproteins - metabolism Thermodynamics
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