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Purification and partial characterization of an amp deaminase from the marine invertebrate palaemon serratus


, : Purification and partial characterization of an amp deaminase from the marine invertebrate palaemon serratus. Comparative Biochemistry & Physiology B 88(4): 1071-1076

1. AMP deaminase from Palaemon serratus tail muscle was partially purified by chromatography on cellulose phosphate. 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. The purified prawn muscle AMP deaminase was contaminated by contractile proteins, one of the major contaminants being actin. 4. The enzyme displayed a very high affinity for actomyosin which was only partially abolished by pyrophosphate.

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DOI: 10.1016/0305-0491(87)90007-1


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