Comparisons of the Tryptophan Synthase Inactivating Enzymes with Proteinases from Yeast
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Immunochemical and enzymatic comparisons of the tryptophan synthase alpha subunits from five species of Enterobacteriaceae.
The reactive surface structures of alpha subunits of tryptophan synthase from Escherichia coli, Shigella dysenteriae, Salmonella typhimurium, Aerobacter aerogenes, and Serratia marcescens were compared by measuring (i) their reactivities in micro-complement-fixation assays with antibodies directed specifically to E. coli wild-type alpha subunit, (ii) their reactivities in enzyme neutralization ...
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15 صفحه اولThe Subunit Structure of Tryptophan Synthase from Neurospora crassa*
Tryptophan synthase of Neurospora crassa was purified to electrophoretic homogeneity from the wild type strain 74A which had been derepressed by the presence of 0.5 rnr,r indoleacrylic acid in the growth medium. The isolated material migrated as a single symmetrical peak in the ultracentrifuge with a sedimentation constant of 6.0 S. Gel filtration on Sephadex G-ZOO and conventional sedimentatio...
متن کاملThe subunit structure of tryptophan synthase from Neurospora crassa.
Tryptophan synthase of Neurospora crassa was purified to electrophoretic homogeneity from the wild type strain 74A which had been derepressed by the presence of 0.5 mM indoleacrylic acid in the growth medium. The isolated material migrated as a single symmetrical peak in the ultracentrifuge with a sedimentation constant of 6.0 S. Gel filtration on Sephadex G-200 AND CONVENTIONAL SEDIMENTATION E...
متن کاملA study of two yeast proteinases.
Autolysis is a procedure frequently employed in the isolation of materials from yeast. Although the intracellular yeast proteinases play an important r81e in autolysis, these enzymes have not been characterized by using up to date methods of analysis, and the existing literature concerning yeast proteinases presents conflicting results. In 1917, Dernby (1) reported that yeast contains two prote...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1974
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1974.tb03377.x