Porcine growth hormone: molecular cloning of cDNA and expression in bacterial and mammalian cells.
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.
Kato
Y
Y
Hormone Assay Center, Gunma University, Gunma, Japan.
Shimokawa
N
N
Kato
T
T
Hirai
T
T
Yoshihama
K
K
Kawai
H
H
Hattori
M
M
Ezashi
T
T
Shimogori
Y
Y
Wakabayashi
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D015723:Gene Library; D013006:Growth Hormone / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010903:Pituitary Gland, Anterior / Q000378:metabolism; D011994:Recombinant Proteins / Q000302:isolation & purification; D015183:Restriction Mapping; D013552:Swine
D011994:Recombinant Proteins; D013006:Growth Hormone; D004247:DNA