Fluorescence Studies of Zinc Binding to Beef Liver Glutamate Dehydrogenase.

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Fluorescence studies of coenzyme-binding to beef heart lactic dehydrogenase.

Among the many methods which are available for studying the binding of substances to proteins (l), those applied most commonly for pyridine nucleotide-binding to dehydrogenases have been the spectrophotometric (2) and ultracentrifuge measurements (3). An additional method has been introduced through the observations of Boyer and Theorell (4) who found that reduced diphosphopyridine nucleotide i...

متن کامل

Kinetic studies of dogfish liver glutamate dehydrogenase.

Initial-rate studies were made of the oxidation of L-glutamate by NAD+ and NADP+ catalysed by highly purified preparations of dogfish liver glutamate dehydrogenase. With NAD+ as coenzyme the kinetics show the same features of coenzyme activation as seen with the bovine liver enzyme [Engel & Dalziel (1969) Biochem. J. 115, 621--631]. With NADP+ as coenzyme, initial rates are much slower than wit...

متن کامل

Binding studies of a spin-labelled oxidized coenzyme to bovine-liver glutamate dehydrogenase.

NAD+ with a nitroxide piperidine ring linked to the NH2 group of the adenine possesses full coenzymatic activity with glutamate dehydrogenase. Electron spin resonance spectra in the presence of glutamate dehydrogenase show mixtures of free and strongly immobilized spin-label. Binding studies in phosphate buffer demonstrate: (a) weak binary binding to the enzyme with a dissociation constant in t...

متن کامل

Ox liver glutamate dehydrogenase

1. The effect of pyridoxal 5'-phosphate on the activity of ox liver glutamate dehydrogenase towards different amino acid substrates was investigated. 2. Both alanine and glutamate activities decreased steadily in the presence of pyridoxal 5'phosphate. 3. The alanine/glutamate activity ratio increased as a function of inactivation by pyridoxal 5'-phosphate, indicating that glutamate activity is ...

متن کامل

Demonstration of glutamate dehydrogenase isozymes in beef heart mitochondria.

Glutamate dehydrogenase (GDH) has been purified from beef heart mitochondria and compared with crystalline beef liver GDH. The specific activity of heart GDH was 127 units and of liver GDH 80 units. Heart GDH subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis had a protein corresponding to liver GDH and a smaller molecular weight protein. On agarose gel electrophoresis heart...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Acta Chemica Scandinavica

سال: 1965

ISSN: 0904-213X

DOI: 10.3891/acta.chem.scand.19-0390