1987/12/01 by Hideki Maeda, Ryosuke Hashimoto, Teru Ogura +2 · 2 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #Biology #Chemistry #Cloning (programming) #Computer science #Endoplasmic Reticulum Stress and Disease #Gene #Genetics #Glycan #Glycoprotein #Glycosylation #Glycosylation and Glycoproteins Research #Molecular biology #Mutation #N-linked glycosylation #Ubiquitin and proteasome pathways
paper · doi:10.1016/s0022-2275(20)38574-6
openalex publication_date 1987/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
Apolipoprotein C-III (apoC-III) is a major protein of very low density lipoprotein (VLDL). The apoC-III polypeptide contains a carbohydrate chain containing galactosamine, galactose, and sialic acid attached in O-linkage to a threonine residue at position 74. We have cloned the apoC-III gene from a subject whose serum contained unusually high amounts of apoC-III lacking the carbohydrate moiety (C-III-0). DNA sequence analysis of the cloned gene revealed a single nucleotide substitution (A----G) that encodes an alanine at position 74 instead of the normal threonine. As a result of this amino acid replacement, the mutant apoC-III polypeptide is not glycosylated. The mutation in the apoC-III gene creates a novel AluI site that permits diagnosis of the change by Southern blotting of genomic DNA.