title: Stability and conformation of porcine phosphofructokinase M and L.
abstract: 1. The inactivation of porcine liver enzyme in the presence of urea proceeded more rapidly than that of porcine heart muscle enzyme. 2. The inactivation of both enzymes by urea was protected by allosteric activators, but inhibitors had no effect. 3. The circular dichroism spectrum of liver enzyme in the near ultraviolet region was markedly affected by urea, whereas that of heart muscle enzyme was not, except for the band at 255 nm.
authors: Institute of High Polymer Research, Faculty of Textile Science and Technology, Shinshu University, Nagano, Japan.
authors: Y
authors: Y
authors: Uchida
authors: T
authors: T
authors: Koyama
authors: A
authors: A
authors: Hachimori
mesh_terms: D000818:Animals; D002942:Circular Dichroism; D004229:Dithiothreitol / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D011487:Protein Conformation; D013552:Swine; D014508:Urea / Q000494:pharmacology
chemical_list: D007527:Isoenzymes; D014508:Urea; D004492:Edetic Acid; D010732:Phosphofructokinase-1; D004229:Dithiothreitol