Purification and Substrate Specificity of Bovine Liver-Ferrochelatase

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

Purification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain.

A substrate-specific calmodulin-dependent myosin light-chain kinase (MLCK) was purified 45,000-fold to near homogeneity from bovine brain in 12% yield. Bovine brain MLCK phosphorylates a serine residue in the isolated turkey gizzard myosin light chain (MLC), with a specific activity of 1.8 mumol/min per mg of enzyme. The regulatory MLC present in intact gizzard myosin is also phosphorylated by ...

متن کامل

Purification and Substrate Specificity of Arginyl-ribonucleic Acid Synthetase from Rat Liver.

It is generally accepted that in the first phase of protein biosynthesis, amino acid-specific enzymes, the aminoacyl-ribonucleic acid synthetases, carry out the activation of the various amino acids, and that the exacting specificity of these enzymes extends to the transfer of the amino acid to a particular soluble ribonucleic acid. Several investigators (l-5) have achieved the purification of ...

متن کامل

Ferrochelatase from Rhodopseudomonas sphaeroides: substrate specificity and role of sulfhydryl and arginyl residues.

Purified ferrochelatase (protoheme ferrolyase; EC 4.99.1.1) from the bacterium Rhodopseudomonas sphaeroides was examined to determine the roles of cationic and sulfhydryl residues in substrate binding. Reaction of the enzyme sulfhydryl residues with N-ethylmaleimide or monobromobimane resulted in a rapid loss of enzyme activity. Ferrous iron, but not porphyrin substrate, had a protective effect...

متن کامل

Bovine Liver Aspartyl @ - Hydroxylase PURIFICATION AND

The a-ketoglutarate-dependent dioxygenase, LAsp@-Asn)-&hydroxylase which posttranslationally hydroxylates specific aspartic acid (asparagine) residues within epidermal growth factor-like domains was purified from bovine liver and characterized. A 52kDa and a 56-kDa species of this enzyme, which accounted for 60 and 30% of the total enzymatic activity, respectively, were purified to apparent hom...

متن کامل

Bovine liver fructokinase: purification and kinetic properties.

Fructokinase from beef liver has been purified 2300-fold by acid and heat treatment, ammonium sulfate fractionation, and chromatography on Sephadex G-100, DEAE- and CM-cellulose. The purified enzyme is homogeneous by all criteria examined, has a molecular weight of 56 000, and is a dimer of equal molecular weight subunits. The isoelectric point is 5.7. The Michaelis constant for activation by K...

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: European Journal of Biochemistry

سال: 2005

ISSN: 0014-2956,1432-1033

DOI: 10.1111/j.1432-1033.1982.tb06892.x