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Role of the NH2-terminus and the COOH-end of HU-IFN-gamma for structure and activity

 
: Boehm, J.; Otto, B.; Roggenthien, J.; Schöne, B.; Slodowski, O.

Journal of Interferon Research (1989), Nr.2, S.180
ISSN: 0197-8357
Meeting on the Interferon System <1989, Florenz>
Englisch
Konferenzbeitrag
Fraunhofer ITA ( ITEM) ()
genetic recombination; genetic technology; interferon gamma; mutant; mutation

Abstract
Hu-rec. IFN-gamma (143 aa) from bacterial cells was purified to more than 95 per cent purity. Due to the protease sensitivity of the COOH-end, rich of clusters of arg and lys, the pure dimeric IFN-gamma was further trimmed to nearly one population of complete, 143 aa long protein. Crystals of IFN-gamma were grown from ammoniumsulfate solutions using the hanging drop method and characterized. They contain indeed IFN-gamma which conserves full antiviral activity. The crystals are larger than 0.2 A resolution. However, they are temperature sensitive and have therefore to be cooled during x-ray analysis. First structural data may be presented.

: http://publica.fraunhofer.de/dokumente/PX-32215.html