Kato Y, Shimokawa N, Kato T, Hirai T, Yoshihama K, Kawai H, Hattori M, Ezashi T, Shimogori Y, Wakabayashi K
Hormone Assay Center, Gunma University, Gunma, Japan.
Biochim Biophys Acta. 1990 Apr 6;1048(2-3):290-3. doi: 10.1016/0167-4781(90)90069-e.
Porcine growth hormone (PGH) precursor cDNAs were cloned from a pituitary cDNA library constructed in lambda gt11 by immunoscreening. One of the three clones characterized contained an entire nucleotide sequence for the 216-amino-acid precursor molecule. The deduced amino-acid sequence of PGH confirmed the sequence previously reported for that of the genomic DNA of PGH except for one base difference in the coding sequence. Expression of the full-length PGH cDNA was achieved in bacteria and mammalian cells. The mammalian cell line, COS-1, produced the GH molecule which processed the signal peptide and had the same molecular weight as standard PGH, in contrast to the higher molecular weight of the bacterial product. Radioimmunoassay of the recombinant PGH produced in COS-1 cells also revealed an inhibition curve similar to that of the standard PGH.
通过免疫筛选从构建于λgt11中的垂体cDNA文库中克隆出猪生长激素（PGH）前体cDNA。所鉴定的三个克隆之一包含了216个氨基酸前体分子的完整核苷酸序列。PGH推导的氨基酸序列除编码序列中有一个碱基差异外，证实了先前报道的PGH基因组DNA序列。全长PGH cDNA在细菌和哺乳动物细胞中实现了表达。与细菌产物较高的分子量相比，哺乳动物细胞系COS-1产生了处理信号肽且与标准PGH分子量相同的GH分子。对COS-1细胞中产生的重组PGH进行放射免疫测定，结果也显示出与标准PGH相似的抑制曲线。
