AMPLIFICATION OF MYOADENYLATE DEAMINASE DURING EVOLUTION .2. PURIFICATION AND PROPERTIES OF THE ENZYME FROM 2 ELASMOBRANCH FISH, SCYLIORHINUS-CANICULA AND RAJA-CLAVATA
Jp. Raffin et al., AMPLIFICATION OF MYOADENYLATE DEAMINASE DURING EVOLUTION .2. PURIFICATION AND PROPERTIES OF THE ENZYME FROM 2 ELASMOBRANCH FISH, SCYLIORHINUS-CANICULA AND RAJA-CLAVATA, Comparative biochemistry and physiology. B. Comparative biochemistry, 106(4), 1993, pp. 999-1007
1. Muscle AMP deaminase was purified from two species of elasmobranch
fish displaying different activities of the enzyme: the dogfish, Scyli
orhinus canicula and the skate, Raja clavata. 2. The effects of pH, mo
novalent cations, inorganic phosphate and nucleotide effectors were st
udied on the two enzyme preparations. 3. While the physicochemical and
regulatory properties of the AMP deaminase of skate muscle were very
similar to those of the higher vertebrate muscle forms, the dogfish en
zyme displayed properties of the non-muscular forms of higher vertebra
tes. 4. These results are discussed in view of the genetic events whic
h have led to the appearance of different AMP deaminase forms from a c
ommon ancestral gene.