TY - JOUR
T1 - A 34-kilodalton polypeptide is associated with 1,3-β-glucan synthase activity from the fungus Saprolegnia monoica
AU - Bulone, Vincent
AU - Fèvre, Michel
PY - 1996/7
Y1 - 1996/7
N2 - Three major polypeptides of 34, 48 and 50 kDa which appear to copurify with 1,3-β-glucan synthase activity were isolated by glycerol gradient centrifugation of Chaps-solubilized proteins from the fungus Saprolegnia monoica. The antiserum produced against the 34-kDa polypeptide revealed by protein immunoblotting that this polypeptide copurified with 1,3-β-glucan synthase during enzyme purification. This antiserum adsorbs the enzyme activity as well as the 48- and 50-kDa polypeptides. These results indicate that the 34-kDa peptide is a component of the multisubunit protein complex involved in 1,3-β-glucan synthase activity.
AB - Three major polypeptides of 34, 48 and 50 kDa which appear to copurify with 1,3-β-glucan synthase activity were isolated by glycerol gradient centrifugation of Chaps-solubilized proteins from the fungus Saprolegnia monoica. The antiserum produced against the 34-kDa polypeptide revealed by protein immunoblotting that this polypeptide copurified with 1,3-β-glucan synthase during enzyme purification. This antiserum adsorbs the enzyme activity as well as the 48- and 50-kDa polypeptides. These results indicate that the 34-kDa peptide is a component of the multisubunit protein complex involved in 1,3-β-glucan synthase activity.
KW - 1,3-β-Glucan synthase
KW - Antibody
KW - Polypeptide
KW - Saprolegnia
UR - http://www.scopus.com/inward/record.url?scp=0030200477&partnerID=8YFLogxK
U2 - 10.1111/j.1574-6968.1996.tb08328.x
DO - 10.1111/j.1574-6968.1996.tb08328.x
M3 - Article
C2 - 8764476
AN - SCOPUS:0030200477
SN - 0378-1097
VL - 140
SP - 145
EP - 150
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
IS - 2-3
ER -