Properties of human hepatoma adenylate kinases. |
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| Authors: | E Cayanis |
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| Affiliation: | 1. Infectious Diseases Department, Laboratory of Experimental Infection, Hospital Universitari de Bellvitge, IDIBELL, Universitat de Barcelona, Barcelona, Spain;2. Department of Clinical Laboratory, Hospital Universitari de Bellvitge, IDIBELL, Universitat de Barcelona, Barcelona, Spain;3. Infection & Immunity Program and Department of Microbiology, Biomedicine Discovery Institute, Monash University, Melbourne, Australia;4. Centro de Investigación Biomédica en Red en Enfermedades Infecciosas (CIBERINFEC), Instituto de Salud Carlos III, Madrid, Spain;1. Key Laboratory of Geotechnical and Underground Engineering of Ministry of Education, Department of Geotechnical Engineering, Tongji University, Shanghai 200092, China;2. Department of Geotechnical Engineering, College of Civil Engineering, Tongji University, Shanghai 200092, China;3. Department of Physical Science and Engineering, Institute of Acoustics, Tongji University, Shanghai 200092, China;4. Wuhan Changsheng Engineering Exploration Technology Development Co., Ltd., Wuhan, Hubei 430312, China |
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| Abstract: | - 1.1. Three adenylate kinase isoenzymes, designated AK I, II and III in order of their increasing electrophoretic mobility towards the anode were partially purified from human hepatomas.
- 2.2. When AK III was passed through phosphocellulose, multiple forms were again obtained.
- 3.3. Starch gel electrophoresis revealed that AK I and AK III C, as well as AK II and AK III B had similar electrophoretic mobilities.
- 4.4. A study of the properties, which included pH optima, acid, alkali and temperature stability studies, substrate analogue utilization and Michaelis constant estimations, showed certain similarities as well as differences between the various adenylate kinases.
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