Yoshida A, Hara T, Ikenaga H, Takeuchi M
Central Laboratories for Key Technology, Kirin Brewery Co., Ltd, Fukuura, Japan.
Glycoconj J. 1995 Dec;12(6):824-828. doi: 10.1007/BF00731244.
By employing a bovine UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyl transferase (O-GalNAc transferase) cDNA as a probe, we isolated four overlapping cDNAs from a porcine lung cDNA library. Both the nucleotide sequence of the porcine cDNA and the predicted primary structure of the protein (559 amino acids) proved to be very similar to those of the bovine enzyme (95% and 99% identity, respectively). Transient expression of the clone in COS-7 cells, followed by enzymatic activity assays, demonstrated that this cDNA sequence encodes a porcine O-GalNAc transferase. The intracellular O-GalNAc transferase activity was increased approximately 100-fold by transfecting cells with the porcine cDNA.
通过使用牛UDP-N-乙酰半乳糖胺：多肽N-乙酰半乳糖胺基转移酶（O-连接N-乙酰半乳糖胺转移酶）cDNA作为探针，我们从猪肺cDNA文库中分离出四个重叠的cDNA。猪cDNA的核苷酸序列和预测的蛋白质一级结构（559个氨基酸）均与牛酶的序列非常相似（分别具有95%和99%的同一性）。该克隆在COS-7细胞中的瞬时表达，随后进行酶活性测定，结果表明该cDNA序列编码一种猪O-连接N-乙酰半乳糖胺转移酶。用猪cDNA转染细胞后，细胞内O-连接N-乙酰半乳糖胺转移酶的活性增加了约100倍。
