Calreticulin Binding Affinity for Glycosylated Laminin
نویسندگان
چکیده
منابع مشابه
Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins.
Calreticulin (CRT) is thought to be a molecular chaperone that interacts with glycoproteins exclusively through a lectin site specific for monoglucosylated oligosaccharides. However, this chaperone function has never been directly demonstrated nor is it clear how lectin-oligosaccharide interactions facilitate glycoprotein folding. Using purified components, we show that CRT suppresses the aggre...
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When brain proteins separated by SDS-polyacrylamide gel electrophoresis (PAGE) and transferred to nitrocellulose are probe with 125I-labeled laminin, a single broad band of approximately 120 kDa binds laminin specifically. We show here by two-dimensional electrophoresis and protein microsequencing that this band consists of two distinct laminin-binding proteins. One of these is the amyloid prec...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.14.7891