By Yu. M. Torchinsky, T. T. Berezov (auth.), Dr. Timo K. Korpela, Prof. Philipp Christen (eds.)
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Extra info for Biochemistry of Vitamin B6 : Proceedings of the 7th International Congress on Chemical and Biological Aspects of Vitamin B6 Catalysis, held in Turku, Finland, June 22–26, 1987
Before The surprise that next I There met his two of the day was laboratory. ahead not young time Congress he not we of came an when began, to old only and my man enjoyed arrived contacted hotel, and me Khomutov in Moscow for including Yurii five months with Torchinsky and his Morozov. One I Marat In 1965 I these men and with Yurii by his to and Karpeisky, both of whom are here today 26 years later. worked him expressed took in conversation but good Radii colleagues, I I others secret of Braunstein's success was his ability to bring together a powerful team of inspire chemically knowledgeable, them to outstanding effort.
COLI OF cDNA OF mAspAT AND pre-mAspAT OF CHICKEN On expression of the cDNA of pre-mAspAT of chicken in E. , 1987). The tendency of the precursor to form aggregates either with itself or more likely with other cellular constituents becomes also evident on sucrose density centrifugation of a precursor containing rabbit reticulocyte lysate programmed with chicken liver mRNA or of a homogenate of cultured chicken embryo fibroblasts that had been treated,with the uncoupling agent carbonyl cyanide m-chlorophenylhydrazone (CCCP).
1981) E. coli DH1 cells transformed with pUC9sGOT produce a hybrid protein, the NH 2 -terminal region of which contains 12 amino acids derived from a-galactosidase. This protein constitutes 15% of the total soluble protein. The purified hybrid protein showed the same catalytic properties (Km and Vmax values) as rat cAspAT. N-terminus In JM109 Thus the of cAspAT did cells, extra not polypeptide alter induced by addition to the the catalytic properties. the plasmid pDK201 expressed a had the same Mr value as cAs pAT activity was attached (Fig.