Slow conformational transitions of muscle glycogen phosphorylase b induced by specific ligands.
The effect of specific ligands (the substrate glucose 1-phosphate, AMP, and flavins) on the initial rate of tryptic digestion of muscle glycogen phosphorylase b has been studied (0.02 M HEPES, pH 6.8; 37 degrees C). Differences were observed between the kinetic curves of the enzyme trypsinolysis initiated by the addition of a trypsin/ligand mixture and once trypsin was added to the enzyme preincubated with a ligand for 10 min. It was suggested that the specific ligands studied induce relatively slow conformational changes in the phosphorylase b molecule.
Kurganov
B I
BI
A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow.
Schors
E I
EI
D000249:Adenosine Monophosphate / Q000378:metabolism; D000494:Allosteric Regulation; D000818:Animals; D018360:Crystallography, X-Ray; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D005415:Flavins / Q000378:metabolism; D005958:Glucosephosphates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D009132:Muscles / Q000201:enzymology*; D006005:Phosphorylases / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D011817:Rabbits; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism
D005415:Flavins; D005958:Glucosephosphates; D005182:Flavin-Adenine Dinucleotide; D000249:Adenosine Monophosphate; C031590:glucose-1-phosphate; D006005:Phosphorylases; D014357:Trypsin