[Subunit structure of AMP-deaminase from skeletal muscles].
AMP-deaminase was purified from skeletal muscle of rat by the affinity chromatography on phosphocellulose and gel-filtration on Sephadex G-200. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate (SDS-PAGE) has shown three protein bands on each step of purification. One of them corresponds to the subunit of tetrameric AMP-deaminase molecule with molecular weight of 76 kDa and two others--to the protein subunit with molecular weight of 42 and 33 kDa. Repeated SDS-PAGE of the main subunit band has revealed again all these protein bands. The data obtained indicate that AMP-deaminase subunit of 76 kDa is able to dissociate on two polypeptide chains with similar values of molecular weights in the presence of SDS.
Aĭrapetian
R L
RL
Mardanian
S S
SS
Arutiunian
A V
AV
D000659:AMP Deaminase / Q000302:isolation & purification*; D000818:Animals; D002384:Catalysis; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009709:Nucleotide Deaminases / Q000302:isolation & purification*; D011487:Protein Conformation; D051381:Rats; D012967:Sodium Dodecyl Sulfate
D012967:Sodium Dodecyl Sulfate; D009709:Nucleotide Deaminases; D000659:AMP Deaminase
Sub''edinichnoe stroenie AMP-dezaminazy skeletnykh myshts.