EXPRESSION OF HUMAN PARATHYROID-HORMONE IN ESCHERICHIA-COLI

被引：17

作者：

HOGSET, A ^{[1
]}

BLINGSMO, OR ^{[1
]}

GAUTVIK, VT ^{[1
]}

SAETHER, O ^{[1
]}

JACOBSEN, PB ^{[1
]}

GORDELADZE, JO ^{[1
]}

ALESTROM, P ^{[1
]}

GAUTVIK, KM ^{[1
]}

机构：

[1] AGR UNIV NORWAY,N-1432 AS,NORWAY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 166卷 / 01期

关键词：

D O I：

10.1016/0006-291X(90)91910-K

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human parathyroid hormone (hPTH) is a peptide hormone consisting of 84 amino acids. Using the expression plasmid pKK223-3 with the strong tac-promoter, we have produced a variant of hPTH in E. coli. From the expression plasmid construct the expected product was hPTH with an N-terminal extension of Met-Gly. The peptide was extracted from E. coli cells and purified by high performance liquid chromatography. In two different gel electrophoresis systems including identification by immunoblotting the product behaved exactly as an hPTH standard. N-terminal amino acid sequence analysis of the purified product showed traces of Gly-hPTH. At least 90% of the expressed product was N-terminally blocked, suggesting the presence of N-formyl-methionine. This variant of hPTH did not stimulate adenylate cyclase activity in rat osteosarcoma cell membranes. © 1990.

引用

页码：50 / 60

页数：11

共 27 条

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[2]

AURBACH GD, 1959, J BIOL CHEM, V234, P3179

[3] HUMAN PREPROPARATHYROID HORMONE SYNTHESIZED IN ESCHERICHIA-COLI IS TRANSPORTED TO THE SURFACE OF THE BACTERIAL INNER MEMBRANE BUT NOT PROCESSED TO THE MATURE HORMONE [J].