1. Studies on the subunit structure of chorismate mutase − prephenate dehydrogenase from Arobacter aerogenes
- Author
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G.L.E. Koch, Denis C. Shaw, and Frank Gibson
- Subjects
Electrophoresis ,Protein Denaturation ,Protein subunit ,Sodium ,Detergents ,Enterobacter ,chemistry.chemical_element ,Naphthalenes ,Dissociation (chemistry) ,chemistry.chemical_compound ,Methionine ,Urea ,Trypsin ,chemistry.chemical_classification ,Prephenate dehydrogenase ,General Medicine ,Sulfuric Acids ,Chorismate Mutase Prephenate Dehydrogenase ,Molecular Weight ,Enzyme ,Biochemistry ,chemistry ,Chorismate mutase ,Sulfonic Acids ,Peptides - Abstract
1. Studies on the properties of dissociated chorismate mutase − prephenate dehydrogenase from Aerobacter aerogenes indicated the presence of subunits. Estimates of the molecular weight of the subunits following dissociation by sodium dodecyl sulphate or erea yielded a value of about 40000 which is half the molecular weight of the native enzyme. Two − dimentional chromatography of dansylated tryptic peptides from the protein also indicated that it consisted of two very similar or identical subunits of about 40000 molecular weight. The amino terminal end group of the protein was found to be methionine.
- Published
- 1970
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