BIOMAT Database Logo BIOMAT Database Logo

Effect of flavins on the rate of proteolytic digestion of muscle glycogen phosphorylase b. 1993

B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
AN Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow.

The kinetics of tryptic proteolysis of rabbit skeletal muscle phosphorylase b has been registered by the diminishing of protein fluorescence intensity at lambda = 335 nm (excitation at 290 nm) or by the disappearance of the enzyme activity (0.02 M Hepes buffer, pH 6.8, 37 degrees C). The first procedure showed that flavins (riboflavin, FMN, FAD) protected the enzyme against tryptic digestion. Microscopic dissociation constants for the complexes of phosphorylase b with riboflavin, FMN and FAD were calculated from dependences of the initial digestion rate on the flavin concentration. They where equal to 30 +/- 1, 15.8 +/- 0.2 and 36 +/- 1 microM, respectively. No influence of FMN on the rate of the tryptic hydrolysis of phosphorylase b was observed when using the second procedure (enzyme activity test). FMN completely prevents the formation of 69-, 81- and 85-kDa fragments during 20 min incubation of phosphorylase b with trypsin.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D010763 Phosphorylase b The inactive form of GLYCOGEN PHOSPHORYLASE that is converted to the active form PHOSPHORYLASE A via phosphorylation by PHOSPHORYLASE KINASE and ATP.
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D005182 Flavin-Adenine Dinucleotide A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972) FAD,Flavitan,Dinucleotide, Flavin-Adenine,Flavin Adenine Dinucleotide
D005415 Flavins Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.
D005486 Flavin Mononucleotide A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues. FMN,Flavin Mononucleotide Disodium Salt,Flavin Mononucleotide Monosodium Salt,Flavin Mononucleotide Monosodium Salt, Dihydrate,Flavin Mononucleotide Sodium Salt,Riboflavin 5'-Monophosphate,Riboflavin 5'-Phosphate,Riboflavin Mononucleotide,Sodium Riboflavin Phosphate,5'-Monophosphate, Riboflavin,5'-Phosphate, Riboflavin,Mononucleotide, Flavin,Mononucleotide, Riboflavin,Phosphate, Sodium Riboflavin,Riboflavin 5' Monophosphate,Riboflavin 5' Phosphate,Riboflavin Phosphate, Sodium
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012256 Riboflavin Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE. Vitamin B 2,Vitamin G,Vitamin B2

Related Publications

B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
Specificity of inhibition of muscle glycogen phosphorylase b by flavins.
March 1995, Biochemistry and molecular biology international,
B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
The interaction of muscle glycogen phosphorylase b with glycogen.
December 1982, Biochimica et biophysica acta,
B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
[Delayed conformational changes of muscle glycogen phosphorylase b, caused by recording the rate of digestion of the enzyme by trypsin].
January 1992, Doklady Akademii nauk,
B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
Effect of arginine on stability and aggregation of muscle glycogen phosphorylase b.
December 2020, International journal of biological macromolecules,
B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
[Effect of specific ligands on heat inactivation of muscle glycogen phosphorylase b].
May 1996, Biokhimiia (Moscow, Russia),
B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
Enzyme kinetics of muscle glycogen phosphorylase b.
October 2007, Biochemistry,
B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
[Binding of muscle phosphorylase B by glycogen].
January 1979, Molekuliarnaia biologiia,
B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
Biospecific affinity chromatography of smooth muscle glycogen phosphorylase b on glycogen--Sepharose.
July 1978, FEBS letters,
B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
[Kinetics of the reaction between muscle glycogen phosphorylase B and glycogen].
January 1980, Molekuliarnaia biologiia,
B I Kurganov, and E I Schors, and N B Livanova, and N A Chebotareva, and T B Eronina, and I E Andreeva, and V P Makeeva, and N D Pekel
[A quantitative method of assessing the strength of binding of a ligand with an enzyme based on proteolytic digestion. Binding of FMN with muscle glycogen phosphorylase B].
January 1991, Doklady Akademii nauk SSSR,
Copied contents to your clipboard!