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Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in vivo and in vitro.
The present study shows that the specific activity of BPGM in erythrocytes of diabetic patients is decreased, compared to normal controls as judged by 2,3-DPG synthetase activity and immunoreactive contents and the loss of enzymatic activity appears to be due to the glycation of Lys158 which may be located in the vicinity of the substrate binding site.
Contents of myofibrillar proteins in cardiac, skeletal, and smooth muscles.
The in situ contents of myosin, actin, alpha-actinin, tropomyos in, troponin, desmin were estimated in dog cardiac, rabbit skeletal, and chicken smooth muscles and dye binding capacity of individual myofibrillar proteins was determined by using the purified protein.
Cardiac myosin from pig heart ventricle. Purification and enzymatic properties.
The purified myosin was free from nucleic acid, actin, tropomyosin, Troponin, the 150,000 molecular weight protein and other contaminants, and the pH-activity profiles and the effects of SH modification were of the skeletalMyosin type except that the activities were lower.
Degradation of rat cardiac myofibrils and myofibrillar proteins by a myosin-cleaving protease.
Cardiac myosin in the filamentous state was more readily degraded with the protease than the myos in the soluble state, and the tropomyosin assembled in myofibrils and actin-tropomyOSin complex were insusceptible to the prote enzyme.
Ultrastructural alteration of rat cardiac myofibrils caused by a myosin-cleaving protease.
When rat cardiac muscle I-Z-I brushes were subjected to proteolysis, the protein.
cDNA encoding type B subunit of rat phosphoglycerate mutase: its isolation and nucleotide sequence.
  • K. Uchida
  • Biology, Chemistry
    Archives of biochemistry and biophysics
  • 1 August 1991