title: [Purification and biological activity of rh-leptin expressed in Escherichia coli].
abstract: The human leptin was successfully expressed with high level in E. coli under the control of PL promotor. The yield of recombinant protein was over 40% of total cellular protein and expressed as inclusion bodies. The recombinant human leptin (rh-leptin) was purified with gel filtration, anion-exchange and reverse chromatography. Refolding was achieved by gradually reducing denaturant using a diafiltration method. The refolded rh-leptin was characterized by SDS-PAGE, Western-blotting and its first 15 amino acid residues sequence of the N-terminal. The purified product was found to be biologically active, reducing the food intake and body weight gain upon testing in BALB/c mice.
authors: Shandong Tumor Biotherapy Centre, Institute of Basic Medicine, Shandong Academy of Medical Sciences, Jinan 250062, China. yrzhao@public.jn.sd.ch
authors: Y R
authors: YR
authors: Zhao
authors: J F
authors: JF
authors: Wang
authors: L
authors: L
authors: You
authors: C Y
authors: CY
authors: Gao
authors: Z G
authors: ZG
authors: Tian
authors: J
authors: J
authors: Zhang
authors: N
authors: N
authors: Han
authors: J
authors: J
authors: Yin
authors: R
authors: R
authors: Sun
mesh_terms: D000818:Animals; D004435:Eating / Q000187:drug effects; D004926:Escherichia coli / Q000235:genetics*; D005260:Female; D006801:Humans; D020738:Leptin / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology; D051379:Mice; D008807:Mice, Inbred BALB C; D011994:Recombinant Proteins / Q000096:biosynthesis*; D015430:Weight Gain / Q000187:drug effects
chemical_list: D020738:Leptin; D011994:Recombinant Proteins