High expression and characterization of human parathyroid hormone in Escherichia coli / 生物工程学报
Chinese Journal of Biotechnology
; (12): 102-106, 2003.
Article
em Zh
| WPRIM
| ID: wpr-259186
Biblioteca responsável:
WPRO
ABSTRACT
Human parathyroid hormone (hPTH) was highly expressed in Escherichia coli by inserted the synthesized whole hPTH cDNA into the vectors pBV220 and pET22b. After expression and disruption, the purified product was acquired through cation exchange chromatography and reverse phase chromatography. From the results of N-terminal sequencing and MALDI-TOF-MS analysis the recombiant prtein was indentified as intact hPTH. In in vitro Bioassays the recombinant hPTH stimulated adenylate cyclase as the standard did. In ovariectomized rats the recombinant hPTH markedly increased the femoral bone mass and bone mineral density.
Texto completo:
1
Índice:
WPRIM
Assunto principal:
Hormônio Paratireóideo
/
Farmacologia
/
Dados de Sequência Molecular
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Sequência de Bases
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Ovariectomia
/
Densidade Óssea
/
Química
/
Cromatografia por Troca Iônica
/
Alinhamento de Sequência
/
Sequência de Aminoácidos
Limite:
Animals
/
Female
/
Humans
Idioma:
Zh
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2003
Tipo de documento:
Article