Properties of native calf spleen NAD+ glycohydrolase immobilized by hydrophobic interaction.
NAD+ glycohydrolase, an amphipathic membrane-bound enzyme, solubilized from calf spleen microsomes with detergents and purified, was immobilized by hydrophobic interactions on octyl-Sepharose. Conditions are described for optimal adsorption on the gel. The immobilized enzyme remained catalytically active (hydrolase and transglycosidase activities) and could be used to prepare nicotinic acid analogs of NAD(P)+.
Muller
H M
HM
Laboratoire de Chimie Enzymatique, CNRS UA 1182, Institut de Botanique, Strasbourg, France.
Schuber
F
F
D000818:Animals; D002384:Catalysis; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003902:Detergents; D004800:Enzymes, Immobilized; D005782:Gels; D008861:Microsomes / Q000201:enzymology; D009244:NAD+ Nucleosidase / Q000302:isolation & purification*; D009249:NADP / Q000096:biosynthesis; D012685:Sepharose; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet; D013154:Spleen / Q000201:enzymology*; D014867:Water
D003902:Detergents; D004800:Enzymes, Immobilized; D005782:Gels; D014867:Water; D009249:NADP; D012685:Sepharose; D009244:NAD+ Nucleosidase