Magnusson R P, Gestautas J, Taurog A, Rapoport B
Department of Medicine, Veterans' Administration Medical Center, San Francisco, California 94121.
J Biol Chem. 1987 Oct 15;262(29):13885-8.
We have isolated and determined the nucleotide sequence of overlapping cDNA clones, representing the entire structural gene for pig thyroid peroxidase. The protein coding region extends from an ATG residue at base 252 to a termination codon at base 3030, coding for a 100.4-kDa apoprotein of 926 amino acids. The derived amino acid composition agrees well with the experimentally determined amino acid composition of purified pig thyroid peroxidase. Five potential glycosylation sites are present in the protein. Potential membrane spanning regions are present at the amino-terminal end (1-23) and near the carboxyl-terminal end (845-870) of the protein. These data indicate that pig thyroid peroxidase is synthesized as a single polypeptide that is membrane-bound.
我们已经分离并确定了重叠cDNA克隆的核苷酸序列，这些克隆代表猪甲状腺过氧化物酶的完整结构基因。蛋白质编码区从第252位碱基的ATG残基延伸至第3030位碱基的终止密码子，编码一个由926个氨基酸组成的100.4 kDa脱辅基蛋白。推导的氨基酸组成与纯化的猪甲状腺过氧化物酶的实验测定氨基酸组成非常吻合。该蛋白质中存在五个潜在的糖基化位点。在蛋白质的氨基末端（1-23）和羧基末端附近（845-870）存在潜在的跨膜区域。这些数据表明猪甲状腺过氧化物酶作为一种膜结合的单一多肽合成。
