Purification and partial characterization of an AMP deaminase from the marine invertebrate Palaemon serratus |
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| Institution: | 1. Centre for Chemical Biology, Universiti Sains Malaysia, Sains@USM, Blok B No. 10, Persiaran Bukit Jambul, 11900 Bayan Lepas, Penang, Malaysia;2. Centre for Marine and Coastal Studies, Universiti Sains Malaysia, 11800 Minden, Penang, Malaysia;3. School of Biological Sciences, Universiti Sains Malaysia, 11800 Minden, Penang, Malaysia;2. Active Living and Rehabilitation: Aotearoa New Zealand, Health and Rehabilitation Research Institute, School of Clinical Sciences, Auckland University of Technology, Northcote, Auckland, New Zealand;3. BioDesign Lab, School of Engineering, Computer and Mathematical Sciences, Auckland University of Technology, Auckland, New Zealand;4. Health and Rehabilitation Research Institute, School of Clinical Sciences, Auckland University of Technology, Auckland, New Zealand;1. ICAR—Directorate of Coldwater Fisheries Research, Bhimtal, 263136 Nainital, Uttarakhand, India;2. Gauhati University, Guwahati, 781014 Assam, India;3. Dera Natung Government College, Itanagar, 791111 Arunachal Pradesh, India |
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| Abstract: | - 1.1. AMP deaminase from Palaemon serratus tail muscle was partially purified by chromatography on cellulose phosphate.
- 2.2. Muscle homogenates expressed very low enzyme activities and the presence of ATP was necessary to detect AMP deaminase. The specific activity and substrate affinity of the purified enzyme were also very low.
- 3.3. The purified prawn muscle AMP deaminase was contaminated by contractile proteins, one of the major contaminants being actin.
- 4.4. The enzyme displayed a very high affinity for actomyosin which was only partially abolished by pyrophosphate.
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