Iranian Biomedical Journal
مجله بیومدیکال ایران
IBJ
Basic Sciences
http://ibj.pasteur.ac.ir
1
admin
1028-852X
2008-823X
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10.61882/ibj
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8888
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en
jalali
1378
4
1
gregorian
1999
7
1
3
3
online
1
fulltext
en
Evidence of Tryptophan at or near Active Site of Glucoamylase I of Arthrobotrys amerospora
مقاله کامل
Full Length/Original Article
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.
Glucoamylase I, Tryptophan, Arthrobotrys amerospora
103
107
http://ibj.pasteur.ac.ir/browse.php?a_code=A-10-1-411&slc_lang=en&sid=1
Dariush
Norouzian
داریوش
نوروزیان