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.
Norouzian,D , Akbarzadeh,A , Rostami,K , Nouri Inanlou,D and Farahmand,B . (1999). Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora. Iranian Biomedical Journal, 3(3), 103-107.
MLA
Norouzian,D , , Akbarzadeh,A , , Rostami,K , , Nouri Inanlou,D , and Farahmand,B . "Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora", Iranian Biomedical Journal, 3, 3, 1999, 103-107.
HARVARD
Norouzian D, Akbarzadeh A, Rostami K, Nouri Inanlou D, Farahmand B. (1999). 'Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora', Iranian Biomedical Journal, 3(3), pp. 103-107.
CHICAGO
D Norouzian, A Akbarzadeh, K Rostami, D Nouri Inanlou and B Farahmand, "Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora," Iranian Biomedical Journal, 3 3 (1999): 103-107,
VANCOUVER
Norouzian D, Akbarzadeh A, Rostami K, Nouri Inanlou D, Farahmand B. Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora. Iranian Biomedical Journal. 1999;3(3):103-107.
Iranian Biomedical Journal