title: Comparative studies on muscle AMP-deaminase--I. Purification, molecular weight, subunit structure and metal content of the enzymes from rat, rabbit, hen, frog and pikeperch.
abstract: 1. AMP-deaminase (EC 3.5.4.6) from skeletal muscle of frog and pikeperch was purified to homogeneity and compared with the homogeneous enzymes purified from rat, rabbit and hen skeletal muscle. 2. Their molecular weight was close to 280,000, every enzyme consisted of four identical subunits of molecular weight about 70,000. 3. All enzymes were found to contain about two atoms of zinc per molecule. 4. Minor differences of u.v.-absorption spectra between amphibian and fish muscle enzyme as compared with mammalian and bird muscle enzyme were found.
mesh_terms: D000659:AMP Deaminase / Q000302:isolation & purification*; D000818:Animals; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005399:Fishes; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009709:Nucleotide Deaminases / Q000302:isolation & purification*; D011817:Rabbits; D011893:Rana esculenta; D051381:Rats; D013045:Species Specificity; D013056:Spectrophotometry, Ultraviolet; D015032:Zinc / Q000032:analysis*
chemical_list: D046911:Macromolecular Substances; D009709:Nucleotide Deaminases; D000659:AMP Deaminase; D015032:Zinc