Polypeptide binding properties of the chaperone calreticulin.
Calreticulin is a highly conserved eukaryotic ubiquitious protein located mainly in the endoplasmic reticulum. Two major characteristics of calreticulin are its chaperone activity and its lectin properties, but its precise function in intracellular protein and peptide processing remains to be elucidated. We have investigated the interactions of human calreticulin with denatured ovalbumin, proteolytic digests of ovalbumin, and different available peptides by solid phase assays, size-exclusion chromatography, capillary electrophoresis, and MS. The results show that calreticulin interacts better with unfolded ovalbumin than with native ovalbumin, that calreticulin strongly binds components in proteolytic digests of denatured ovalbumin, and that calreticulin interacts strongly with certain synthetic peptides.
Jørgensen
C S
CS
Department of Protein Chemistry, Statens Serum Institut, Copenhagen, Denmark.
Heegaard
N H
NH
Holm
A
A
Højrup
P
P
Houen
G
G
D000595:Amino Acid Sequence; D019921:Biotinylation; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D037282:Calreticulin; D002850:Chromatography, Gel; D019075:Electrophoresis, Capillary; D004591:Electrophoresis, Polyacrylamide Gel; D019286:Endopeptidase K / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D006358:Hot Temperature; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D008969:Molecular Sequence Data; D010047:Ovalbumin / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D010920:Placenta / Q000737:chemistry; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D012261:Ribonucleoproteins / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013997:Time Factors
D002135:Calcium-Binding Proteins; D037282:Calreticulin; D018832:Molecular Chaperones; D010455:Peptides; D012261:Ribonucleoproteins; D010047:Ovalbumin; D019286:Endopeptidase K