Isolation and sequence determination of two pyridoxal 5'-phosphate-labeled thermolysin peptides from pig muscle phosphoglucose isomerase.

نویسندگان

  • R H Palmieri
  • D M Gee
  • E A Noltmann
چکیده

Pig muscle phosphoglucose isomerase modified with pyridoxal 5'-phosphate under conditions that cause at least 90% inactivation of its catalytic activity was found to incorporate about 1.5 eq of pyridoxal 5'-phosphate per subunit. After digestion with thermolysin, two pyridoxal 5'-phosphate-containing peptides were isolated and their amino acid sequences were determined to be Leu-Gly-pyridoxyl-Lys-Gln and Ile-Ala-Ser-pyridoxyl-Lys-Thr.

برای دانلود 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

Isolation of Crystalline Phosphoglucose Isomerase from Brewers' Yeast.

In a program to elucidate the mechanism by which phosphoglucose isomerasel participates in the catalyzed isomerization between glucose 6-phosphate and fructose g-phosphate, isolation of the enzyme from several sources is pursued as the basis for quantitative studies of its protein nature. The comparative investigation of several heteroenzymes appears to be a valuable tool in identifying the str...

متن کامل

Function of the phosphate group of pyridoxal 5'-phosphate in the glycogen phosphorylase reaction.

To understand the catalytic mechanism of glycogen phosphorylase (EC 2.4.1.1), pyridoxal(5')phospho(1)-beta-D-glucose was synthesized and examined as a hypothetical intermediate in the catalysis. Pyridoxal phosphoglucose bound stoichiometrically to the cofactor site of rabbit muscle phosphorylase b in a similar mode of binding to the natural cofactor, pyridoxal 5'-phosphate. The rate of binding ...

متن کامل

Arginine Decarboxylase from Escherichia coli

A total of three pyridoxyl-peptides were isolated from the inducible argmine decarboxylase of Escherichia coli B following reduction with NaBH4 and proteolysis with trypsin or chymotrypsin. Sodium borohydride reduces the Schiff base formed between pyridoxal-5’-P and the e-amino group of a lysyl residue of the protein. The sequence analysis of the three peptides is consistent with a unique pyrid...

متن کامل

THE JOURNALS OF BIOLOGICAL C~remsm~

A total of three pyridoxyl-peptides were isolated from the inducible argmine decarboxylase of Escherichia coli B following reduction with NaBH4 and proteolysis with trypsin or chymotrypsin. Sodium borohydride reduces the Schiff base formed between pyridoxal-5’-P and the e-amino group of a lysyl residue of the protein. The sequence analysis of the three peptides is consistent with a unique pyrid...

متن کامل

Subunit and peptide compositions of yeast phosphoglucose isomerase isoenzymes.

Three isoenzymes of yeast phosphoglucose isomerase were studied by physical and chemical methods to establish their subunit properties and to identify the structural differences among them which give rise to their heterogeneous chromatographic behavior. Equilibrium sedimentation ultracentrifugation in 6 M guanidine hydrochloride and polyacrylamide gel electrophoresis in the presence of sodium d...

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

برای دانلود 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

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 257 14  شماره 

صفحات  -

تاریخ انتشار 1982