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Incorporation of [ 3 H]glucosamine into keratin‐related polypeptides in pig epidermis
Author(s) -
King Ian A.
Publication year - 1986
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(86)80581-6
Subject(s) - keratin , epidermis (zoology) , glucosamine , biochemistry , chemistry , labelling , tunicamycin , carbohydrate , immunoprecipitation , electrophoresis , glycation , microbiology and biotechnology , biology , anatomy , paleontology , receptor , unfolded protein response , endoplasmic reticulum , gene
Metabolic labelling studies have provided evidence for glycosylated keratins in cultured pig epidermis. [ 3 H]Glucosamine was incorporated into five major particulate polypeptides of M r 68000, 61000, 57000, 53 000 and 48 000. Radioactivity was present in protein‐bound carbohydrate. Non‐enzymic glycation was excluded. Labelling was largely unaffected by tunicamycin indicating that radioactivity was incorporated mainly into O ‐linked oligosaccharides. These [ 3 H]glucosamine‐labelled components were closely related to keratins since (i) they had a similar electrophoretic mobility to polypeptides of purified pig prekeratin, (ii) they were immunoprecipitated by anti‐prekeratin serum and (iii) they were incorporated into reconstituted, intermediate‐sized, keratin filaments.