Isolation, purification and characterization of a trypsin from the pyloric ceca of mullet (Mugil cephalus)

N. Guizani, R. S. Rolle, M. R. Marshall*, C. I. Wei

*المؤلف المقابل لهذا العمل

نتاج البحث: المساهمة في مجلةمراجعة النظراء

34 اقتباسات (Scopus)

ملخص

1. 1. A protease classified as trypsin on the basis of its mol. wt of 24,000, its ability to hydrolyze synthetic substrates N-α-benzoyl-arginine-p-nitroanilide (BAPA) and tosylarginine methyl ester (TAME), and the inhibitory effects of methyl sulfonyl fluoride (PMSF), SBTI, aprotinin and benzamidine on its activity was isolated from the pyloric ceca of mullet. 2. 2. The enzyme exhibited optimal activity at pH 8 and a temperature of 55°C and was stable in the pH range of 7.5-9.0. The Arrhenius energy of activation (Ea) for BAPA hydrolysis by this enzyme was 7.4 kcal/mol. 3. 3. The enzyme showed greater affinity for TAME (K′m = 0.19 mM) as a substrate than for BAPA (K′m = 0.49 mM), and preferential hydrolysis of ester bonds (Vmax = 2640 TAME units/μmmol enzyme) than amide bonds (Vmax = 400 BAPA units/μmol enzyme).

اللغة الأصليةEnglish
الصفحات (من إلى)517-521
عدد الصفحات5
دوريةComparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
مستوى الصوت98
رقم الإصدار4
المعرِّفات الرقمية للأشياء
حالة النشرPublished - 1991

ASJC Scopus subject areas

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