Purification of NAD glycohydrolase from Neurospora crassa conidia by a polyclonal immunoadsorbent.
NAD glycohydrolase from Neurospora crassa conidia was purified by affinity chromatography on a column of polyclonal antibodies bound to an agarose matrix. The procedure was easy, non-denaturating and suitable for repetitive use of the gel. The enzyme obtained appeared homogeneous by sodiumdodecyl sulphate-polyacrylamide gel electrophoresis.
Pace
M
M
Dipartimento di Scienze e Tecnologie Biomediche, University of Milan, Italy.
Agnellini
D
D
Lippoli
G
G
Pietta
P G
PG
Mauri
P L
PL
Cinquanta
S
S
D000818:Animals; D000906:Antibodies / Q000276:immunology; D002846:Chromatography, Affinity / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D009699:N-Glycosyl Hydrolases / Q000276:immunology / Q000302:isolation & purification*; D009244:NAD+ Nucleosidase; D009492:Neurospora crassa / Q000032:analysis / Q000201:enzymology*; D012685:Sepharose
D000906:Antibodies; D012685:Sepharose; D009699:N-Glycosyl Hydrolases; D009244:NAD+ Nucleosidase