| Literature DB >> 1592122 |
M P Schlunegger1, N Cerletti, D A Cox, G K McMaster, A Schmitz, M G Grütter.
Abstract
Recombinant human transforming growth factor beta 2 (TGF-beta 2) was cloned and expressed in E. coli. The protein was isolated from inclusion bodies, renatured and purified to a single component as judged by reversed-phase HPLC. The recombinant TGF-beta 2 was shown to have a biological activity equal to that of native TGF-beta 2 in a fibroblast migration assay. Pure, active recombinant TGF-beta 2 has been crystallized from polyethylene glycol 400. The trigonal crystals of spacegroup P3(1)21 or P3(2)21 have unit cell dimensions of a=b=60.6 A, c=75.2 A and diffract beyond 2.0 A.Entities:
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Year: 1992 PMID: 1592122 DOI: 10.1016/0014-5793(92)80484-x
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124