The Carboxyl - terminal Structure of Rabbit Liver Aldolase

نویسنده

  • B. L. HORECKER
چکیده

The amino acid residues in the carboxyl-terminal region of fructose diphosphate aldolase isolated from fresh rabbit liver are -(Gly,Phe,Leu,Ala,Thr2,Ser2)-Tyr. This differs from the carboxyl-terminal structure in aldolase isolated from tissue which had been frozen and thawed. Amino acid analyses, ultracentrifugation, and digestion with carboxypeptidase suggest that the difference is the result of a limited carboxypeptidase-like proteolytic digestion promoted by the freezing and thawing procedures.

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The carboxyl-terminal structure of rabbit liver aldolase (aldolase B).

The amino acid residues in the carboxyl-terminal region of fructose diphosphate aldolase isolated from fresh rabbit liver are -(Gly,Phe,Leu,Ala,Thr2,Ser2)-Tyr. This differs from the carboxyl-terminal structure in aldolase isolated from tissue which had been frozen and thawed. Amino acid analyses, ultracentrifugation, and digestion with carboxypeptidase suggest that the difference is the result ...

متن کامل

Studies on the Carboxyl- and Amino-terminal Residues of Rabbit Muscle Aldolase.

Many biologically active proteins have been found to contain more than one polypeptide chain, and in most of these proteins the chains appear to be held together in the active structure without the participation of covalent bonds. In these cases relatively mild conditions, presumably too mild to break covalent bonds, will cause dissociation of the protein into its component peptide chains (stru...

متن کامل

Comparative Studies of Liver and Muscle Aldolase. Ii. Immunochemical and Chromatographic Differentiation.

Crystalline fructose diphosphate aldolase preparations obtained from rabbit muscle and bovine liver differ in catalytic efficiency (fructose diphosphate cleavage activity of muscle aldolase is about 10 times that of the liver enzyme) and substrate specificity (the fructose diphosphate to fructose l-phosphate activity ratio is 50 for muscle and 1 for liver aldolase) (2). In spite of these distin...

متن کامل

Tyrosine nitration impairs mammalian aldolase A activity.

Protein tyrosine nitration increases in vivo as a result of oxidative stress and is elevated in numerous inflammatory-associated diseases. Mammalian fructose-1,6-bisphosphate aldolases are tyrosine nitrated in lung epithelial cells and liver, as well as in retina under different inflammatory conditions. Using two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization ti...

متن کامل

Purification and properties of the native form of rabbit liver aldolase. Evidence for proteolytic modification after tissue extraction.

Aldolase was purified from rabbit liver by affinity-elution chromatography. By taking precautions to avoid rupture of lysosomes during the isolation procedure, a stable form of liver aldolase was obtained. The stable form of the enzyme had a specific activity with respect to fructose 1,6-bisphosphate cleavage of 20-28 mumol/min per mg of protein and a fructose 1,6-bisphosphate cleavage of 20-28...

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

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2003