@ARTICLE{Norouzian, author = {Norouzian, Dariush and Akbarzadeh, Azim and Rostami, Khosrow and Nouri Inanlou, Davoud and Farahmand, Behrokh and }, title = {Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora}, volume = {3}, number = {3}, abstract ={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. }, URL = {http://ibj.pasteur.ac.ir/article-1-843-en.html}, eprint = {http://ibj.pasteur.ac.ir/article-1-843-en.pdf}, journal = {Iranian Biomedical Journal}, doi = {}, year = {1999} }