Purification of the ADP-ribosylating enzyme from S. solfataricus by SDS-polyacrylamide gel electrophoresis and electroelution.
The ADPribosylating enzyme from the thermophilic archaeon S. solfataricus was purified by a simple procedure which included preparative electrophoresis on a 0.1% SDS- polyacrylamide gel. The gel slice containing the enzymatic protein was cut out and the enzyme was solubilized by electroelution. The pure enzyme was obtained by chromatography of the electroeluted sample on a DNA-Sepharose column. The purified enzyme retained both its full activity and the structuring ability as a function of temperature increase.
Faraone-Mennella
M R
MR
Dipartimento di Chimica Organica e Biologica Universita' Federico II, Napoli, Italy.
Discenza
A
A
Gambacorta
A
A
Nicolaus
B
B
Farina
B
B
D019843:Archaeal Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D008970:Molecular Weight; D011065:Poly(ADP-ribose) Polymerases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D016944:Sulfolobus / Q000201:enzymology*; D013696:Temperature
D019843:Archaeal Proteins; D011065:Poly(ADP-ribose) Polymerases