Immunoaffinity Purification and Identification of the Molecular Chaperone Calnexin
نویسندگان
چکیده
منابع مشابه
Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function.
Calnexin is a Ca2+-binding transmembrane chaperone of the endoplasmic reticulum that recognizes Glc1Man5-9GlcNAc2 oligosaccharides on folding glycoproteins as well as non-native elements of the polypeptide backbone. This latter mode of recognition enables calnexin to suppress the aggregation of both glycosylated and nonglycosylated substrates. The luminal portion of calnexin (S-Cnx) consists of...
متن کاملThe molecular chaperone calnexin interacts with the NSP4 enterotoxin of rotavirus in vivo and in vitro.
Calnexin is an endoplasmic reticulum (ER)-associated molecular chaperone proposed to promote folding and assembly of glycoproteins that traverse the secretory pathway in eukaryotic cells. In this study we examined if calnexin interacts with the ER-associated luminal (VP7) and transmembrane (NSP4) proteins of rotavirus. Only glycosylated NSP4 interacted with calnexin and did so in a time-depende...
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We have developed a phytochrome immunoaffinity purification procedure that yields undegraded oat (Avena sativa L., cv. Garry) phytochrome of greater than 98% purity within 2 hours when starting with a brushite-purified preparation. Immunoaffinity-purified phytochrome, except for its greater purity, is indistinguishable from conventionally purified phytochrome by gel exclusion chromatography, is...
متن کاملA nucleolar protein allows viability in the absence of the essential ER-residing molecular chaperone calnexin.
In fission yeast, the ER-residing molecular chaperone calnexin is normally essential for viability. However, a specific mutant of calnexin that is devoid of chaperone function (Deltahcd_Cnx1p) induces an epigenetic state that allows growth of Schizosaccharomyces pombe without calnexin. This calnexin-independent (Cin) state was previously shown to be mediated via a non-chromosomal element exhibi...
متن کاملMolecular Chaperone Calnexin Regulates the Function of Drosophila Sodium Channel Paralytic
Neuronal activity mediated by voltage-gated channels provides the basis for higher-order behavioral tasks that orchestrate life. Chaperone-mediated regulation, one of the major means to control protein quality and function, is an essential route for controlling channel activity. Here we present evidence that Drosophila ER chaperone Calnexin colocalizes and interacts with the α subunit of sodium...
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ژورنال
عنوان ژورنال: Bioscience, Biotechnology, and Biochemistry
سال: 1999
ISSN: 0916-8451,1347-6947
DOI: 10.1271/bbb.63.1491