Study of the nature of the binding of phosphate residues in the phosphorylated form of succinyl-CoA synthetase from pigeon breast muscle
The hydrolytic stability of the phosphorylated protein was investigated within a wide pH range. It was shown that the bond of the phosphate residue to protein in complex I is hydrolyzed at alkaline pH values (11.0 and 13.0). At acid pH values this bond is 50% hydrolyzed. The bond of the phosphate residue to protein in complex II is hydrolyzed at acid pH values and is stable at alkaline pH values of the medium. The phosphorylation reaction of the enzyme I, both with hydroxylamine and with diisopropyl fluorophosphate, led to 50% dephosphorylation of the protein. An analysis of an alkaline hydrolysate (3 N NaOH, 3 h, 100/sup 0/C) of the radioactive phosphorylated enzyme II by ion exchange chromatography showed that the radioactive label of the protein is distributed in the fractions of 1-N- and 3-N-phosphohistidine, as well as 1,3-N-diphosphohistidine. The data obtained suggested that phosphate in the phosphorylated enzyme I is bound to protein, with the formation of acyl phosphate and phosphoester bonds. Phosphate in the phosphorylated enzyme II is bound to protein with the formation of a phosphoamide bond.
- Research Organization:
- Lomonosov Moscow State Univ., Moscow (Russian Federation)
- OSTI ID:
- 5879109
- Journal Information:
- Biochemistry (Engl. Transl.); (United States), Vol. 51:7; Other Information: Translated from Biokhimiya; 51: No. 7, 1066-1071(Jul 1986)
- Country of Publication:
- United States
- Language:
- English
Similar Records
Phosphorylation and modulation of enzymic activity of native and protease cleaved purified hepatic 3-hydrox-3-methyl-glutaryl coenzyme A (HMG-CoA) reductase by a calcium, calmodulin-dependent kinase
Zinc ions and alkaline pH alter the phosphorylation state of human erythrocyte membrane proteins
Related Subjects
LIGASES
PHOSPHORYLATION
PHOSPHATES
BINDING ENERGY
HYDROLYSIS
RADIOENZYMATIC ASSAY
PHOSPHOTRANSFERASES
ENZYME ACTIVITY
PROTEINS
ATP
BIOCHEMICAL REACTION KINETICS
CHEMICAL BONDS
ION EXCHANGE CHROMATOGRAPHY
LABELLED COMPOUNDS
LABELLING
MUSCLES
PH VALUE
PHOSPHORUS 32
PIGEONS
STABILITY
SUCCINIC ACID
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIRDS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
CHROMATOGRAPHY
DAYS LIVING RADIOISOTOPES
DECOMPOSITION
DICARBOXYLIC ACIDS
ENERGY
ENZYMES
ISOTOPES
KINETICS
LIGHT NUCLEI
LYSIS
NUCLEI
NUCLEOTIDES
ODD-ODD NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
PHOSPHORUS COMPOUNDS
PHOSPHORUS ISOTOPES
PHOSPHORUS-GROUP TRANSFERASES
RADIOISOTOPES
REACTION KINETICS
SEPARATION PROCESSES
SOLVOLYSIS
TRANSFERASES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques