Denaturation by guanidinium chloride of dimeric MM-creatine kinase and its proteinase K-nicked form: evidence for a multiple-step process-Reference-Cited by-同舟云学术

Denaturation by guanidinium chloride of dimeric MM-creatine kinase and its proteinase K-nicked form: evidence for a multiple-step process

Published:1997-03 Issue:1 Volume:1338 Page:37-46
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Clottes Eric,Leydier Chantal,Couthon Fabienne,Marcillat Olivier,Vial Christian

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference36 articles.

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2. Fritz-Wolf, K., Schnyder, T., Wallimann, T. and Kabsch, W. (1996) Nature 381, 341–345.

3. Mahowald, T.A., Noltmann, E.A. and Kuby, S.A. (1962) J. Biol. Chem. 237, 1535–1548.

4. Messmer, C.H. and Kägi, H.R. (1985) Biochemistry 24, 7172–7178.

5. Morris, G.E. and Jackson, P.J. (1991) Biochem. J. 280, 809–811.

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1. Despite its high similarity with monomeric arginine kinase, muscle creatine kinase is only enzymatically active as a dimer;Archives of Biochemistry and Biophysics;2007-02

2. The evolution from asparagine or threonine to cysteine in position 146 contributes to generation of a more efficient and stable form of muscle creatine kinase in higher vertebrates;The International Journal of Biochemistry & Cell Biology;2006-01

3. Denaturant sensitive regions in creatine kinase identified by hydrogen/deuterium exchange;Rapid Communications in Mass Spectrometry;2005

4. Conformational Dynamics of the GdmHCl-Induced Molten Globule State of Creatine Kinase Monitored by Hydrogen Exchange and Mass Spectrometry;Biochemistry;2004-04-02

5. Hydrogen/deuterium exchange studies of native rabbit MM-CK dynamics;Protein Science;2004-02-01