%0 Journal Article %A Norouzian, Dariush %A Akbarzadeh, Azim %A Rostami, Khosrow %A Nouri Inanlou, Davoud %A Farahmand, Behrokh %T Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora %J Iranian Biomedical Journal %V 3 %N 3 %U http://ibj.pasteur.ac.ir/article-1-843-en.html %R %D 1999 %K Glucoamylase I, Tryptophan, Arthrobotrys amerospora, %X Arthrobotrysamerospora (ATCC 34468) produced glucoamylase in a semi-synthetic medium containing starch as a sole carbon source. Polyacrylamide gel electrophoresis of crude glucoamylase showed three isoenzymes. They were designated as glu I, glu II and glu III according to their electrophoretic mobility. These iso-glucoamylases were purified by column chromatography using DEAE-Sephadex A-50. The major fraction, namely glu I, was subjected to various group specific reagents like NEM, idoacetamide, PALP, DEP, Rose Bengal, NBS and acarbose. N-bromosuccinimide and acarbose totally inhibited glu I. Hg2+ ion did not inhibit glu I activity at 25 m mol concentration. Glu I also showed raw starch activity. %> http://ibj.pasteur.ac.ir/article-1-843-en.pdf %P 103-107 %& 103 %! %9 Full Length/Original Article %L A-10-1-411 %+ %G eng %@ 1028-852X %[ 1999