Preparation of deglycosylated egg white avidin.
A simple procedure for the preparation of deglycosylated avidin is described. Commercially obtained avidin was treated with a mixed microbial culture. The cells were capable of growing on the oligosaccharide residues, but generally ignored the polypeptide portion of the egg white glycoprotein. The resultant deglycosylated avidin retained its biotin-binding characteristics. The major bacterial strain (strain BECH080), responsible for the deglycosylation, was isolated. On the basis of elementary biochemical tests, fatty acid, and phenotypic analyses, the isolate was identified as a strain of Flavobacterium meningosepticum. The primary enzymatic activity that caused the removal of the oligosaccharide residues of avidin appeared to be similar to endoglycosidase F.
Bayer
E A
EA
Department of Biophysics, Weizmann Institute of Science, Rehovot, Israel.
De Meester
F
F
Kulik
T
T
Wilchek
M
M
D001360:Avidin / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D001710:Biotin / Q000378:metabolism; D002846:Chromatography, Affinity; D003208:Concanavalin A; D004529:Egg White / Q000032:analysis*; D005417:Flavobacterium / Q000201:enzymology; D006031:Glycosylation; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000378:metabolism
D003208:Concanavalin A; D001360:Avidin; D001710:Biotin; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase