Efficient purification of recombinant human tumor necrosis factor beta from Escherichia coli yields biologically active protein with a trimeric structure that binds to both tumor necrosis factor receptors-Reference-Cited by-同舟云学术

Efficient purification of recombinant human tumor necrosis factor beta from Escherichia coli yields biologically active protein with a trimeric structure that binds to both tumor necrosis factor receptors

Published:1991-02 Issue:6 Volume:266 Page:3863-3869
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Schoenfeld H J,Poeschl B,Frey J R,Loetscher H,Hunziker W,Lustig A,Zulauf M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference43 articles.

1. Human tumour necrosis factor: precursor structure, expression and homology to lymphotoxin

2. Primary structure of human lymphotoxin derived from 1788 lymphoblastoid cell line.

3. Cloning and expression of cDNA for human lymphotoxin, a lymphokine with tumour necrosis activity

4. Structure of human tumor necrosis factor .alpha. derived from recombinant DNA

5. High-level expression, purification, and characterization of recombinant human tumor necrosis factor synthesized in the methylotrophic yeast Pichia pastoris

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