A spectrophotometric study of vitamin B2 and its coenzyme forms binding to muscle glycogen phosphorylase b.
The vitamin B2 and its coenzyme forms binding to glycogen phosphorylase b from rabbit skeletal muscle has been studied by the spectrophotometric method. The spectral properties of riboflavin, FMN and FAD bound to muscle glycogen phosphorylase b were found to be identical at the wavelengths of 300 to 500 nm. According to data on spectrophotometric titration of muscle glycogen phosphorylase b by FMN, each subunit of the enzyme contains one flavin-binding site.
D000818:Animals; D005486:Flavin Mononucleotide / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D010763:Phosphorylase b / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D012256:Riboflavin / Q000378:metabolism*; D013053:Spectrophotometry / Q000379:methods
D005182:Flavin-Adenine Dinucleotide; D005486:Flavin Mononucleotide; D010763:Phosphorylase b; D006005:Phosphorylases; D012256:Riboflavin