Human Liver Catalase: Cloning, Expression and Characterization of Monoclonal Antibodies

We isolated a cDNA encoding liver catalase from a human liver cDNA library. The cDNA had a high degree of sequence similarity to the corresponding enzyme from other sources. It was expressed in E. coli using the pET15b vector. The protein produced was enzymatically active after purification, and its...

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Bibliographic Details
Published in:Molecules and cells 2003, 15(3), , pp.381-386
Main Authors: Jin, L.H, Kim, D.W, Eum, W.S, Yoon, C.S, Jang, S.H, Choi, H.S, Choi, S. H, Kim, Y.H, Kim, S.Y, Jung, M.R, Park, J.S, Choi, S.Y, Kang, T.C, Choi, M.H, Won, M.H, Lee, K.S. (Hallym University, Chunchon, Republic of Korea)(Lee, H.Y. (Kangwon National University, Chunchon, Republic of Korea), Kang, J.H. (Chongju University, Chongju, Republic of Korea), Kwon, O.S. (Kyungpook National University, Daegu, Republic of Korea), Cho, S.W. (University of Ulsan collegd of Medicine, Seoul, Republic of Korea)
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies, Monoclonal - biosynthesis
Antibodies, Monoclonal - genetics
CATALASE
Catalase - genetics
Catalase - immunology
Catalase - isolation & purification
Cell Line
Cloning, Molecular
Cross Reactions
Escherichia coli - genetics
Gene Library
Humans
Liver - enzymology
Mice
Molecular Sequence Data
MONOCLONAL ANTIBODIES
Rats
Sequence Alignment
생물학
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Summary:We isolated a cDNA encoding liver catalase from a human liver cDNA library. The cDNA had a high degree of sequence similarity to the corresponding enzyme from other sources. It was expressed in E. coli using the pET15b vector. The protein produced was enzymatically active after purification, and its kinetic parameters closely resembled those of other mammalian catalases.
ISSN:1016-8478
0219-1032
DOI:10.1016/S1016-8478(23)13754-X