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Prosomes, small cytoplasmic RNP particles, contain glycoproteins
Author(s) -
Tomek Wolfgang,
Adam Günter,
Schmid Hans-Peter
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80564-7
Subject(s) - glycoprotein , agglutinin , biology , concanavalin a , cytoplasm , glycosylation , biochemistry , n acetylglucosamine , lectin , limulus , enzyme , paleontology , in vitro
Prosomes, ubiquitous small ribonucleoprotein complexes, were isolated from the cytoplasm of erythropoietic mouse cells induced by Friend leucemia virus. We present evidence that some of the prosomal proteins are glycosylated. Specific reactions with the biotinylated lectins concanavalin agglutinin (Con A), Solanum tuberosum agglutinin (STA) and Limulus polyphemus agglutinin (LPA) indicate that the carbohydrate moieties contain N ‐acetylneuraminic acid, N ‐acetylglucosamine and mannosyl‐ or glucosyl‐residues. Glycosylation of prosomal proteins could explain the resistance of prosomes to proteinase K digestion.