PARTIAL PURIFICATION AND BIOLOGICAL ACTIVITY OF THE PRODUCT OF CHEMICALLY SYNTHESIZED HUMAN GROWTH HORMONE GENE EXPRESSION IN ESCHERICHIA COLI

PARTIAL PURIFICATION AND BIOLOGICAL ACTIVITY OF THE PRODUCT OF CHEMICALLY SYNTHESIZED HUMAN GROWTH HORMONE GENE EXPRESSION IN ESCHERICHIA COLI

The product of chemically synthesized human growth hormone gene expression in Escherichia coli was partially purified and proved to be identical with human growth hormone in size, in mobility on non-denaturing polyacrylamide gel electrophoresis, in behabior on HPLC, in immunological properties, and...

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Veröffentlicht in:Chemical & pharmaceutical bulletin 1985/08/25, Vol.33(8), pp.3561-3563
Hauptverfasser: Oshizawa, Tadashi, Terao, Tadao, Sato, Hiroshi, Kimura, Toshio, Fukuda, Hideo, Tanimoto, Tsuyoshi, Niimi, Shingo, Kawamura, Jiro, Hayakawa, Takao, Otsuka, Eiko, Ikehara, Morio
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Chemical Phenomena
Chemistry
Escherichia coli
Escherichia coli - genetics
Genes, Synthetic
growth hormone
Growth Hormone - chemical synthesis
Growth Hormone - pharmacology
Humans
Rats
Recombinant Proteins
tibia test
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Zusammenfassung:The product of chemically synthesized human growth hormone gene expression in Escherichia coli was partially purified and proved to be identical with human growth hormone in size, in mobility on non-denaturing polyacrylamide gel electrophoresis, in behabior on HPLC, in immunological properties, and in biological activity in hypophysectomized rats.
ISSN:0009-2363
1347-5223
DOI:10.1248/cpb.33.3561