Characterization of fish acid proteases by substrate-gel electrophoresis

被引:66
作者
Díaz-López, M
Moyano-López, FJ
Alarcón-López, FJ
García-Carreño, FL
del Toro, MAN
机构
[1] Univ Almeria, Dept Biol Aplicada, E-41020 Almeria, Spain
[2] Ctr Invest Biol, La Paz 23000, BCS, Mexico
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1998年 / 121卷 / 04期
关键词
aspartate protease; fish; proteases; pepsin; sparids; polyacrylamide gel electrophoresis; zymogram; digestive enzymes; inhibition; pepstatin A;
D O I
10.1016/S0305-0491(98)10123-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Several analytical techniques based upon the use of substrate-polyacrylamide gel electrophoresis were evaluated to achieve characterization of aspartate proteases in fish stomach. Since aspartate proteases of fish are more stable at high pH than mammalian pepsins, the most accurate technique for activity assessment is electrophoresis at neutral pH and revealing of such activity at low pH with hemoglobin as substrate. The technique is suitable for characterization of proteases and in comparative assessment of acid protease activity in different sparids. (C) 1998 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:369 / 377
页数:9
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