Recombinant human lymphotoxin: Expression in Escherichia coli, purification, and some properties
Journal Article
·
· Biochemistry (New York)
OSTI ID:161891
- State Research Institute of Applied Microbiology, Obolensk (Russian Federation)
Biosynthesis of human lymphotoxin lacking 21 amino acid residues was studied in the recombinant strain Escherichia coli SG20050/pLT21. The main content of the protein was found to be soluble and predominantly located in the cytoplasm of E. coli. Synthesis of soluble recombinant lymphotoxin was maximal under cultivation in Luria broth at 32{degrees}C for 24 h. A method for isolation and purification of the recombinant protein from E. coli was elaborated. The procedure includes gel filtration on Sephadex G-150 and ion-exchange chromatography on DEAE- and CM-Sephadex. The protein was obtained with 97-fold purification and final yield of 62%. The specific activity was 10{sup 8} units per mg protein. Some physicochemical properties of the protein were investigated. 24 refs., 5 figs., 2 tabs.
- OSTI ID:
- 161891
- Journal Information:
- Biochemistry (New York), Journal Name: Biochemistry (New York) Journal Issue: 9 Vol. 60; ISSN 0006-2979; ISSN BIORAK
- Country of Publication:
- United States
- Language:
- English
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