title: Purification and properties of two molecular forms of arginine kinase from the adductor muscle of the scallop, Pecten maximus.
abstract: 1. Two molecular forms of arginine kinase, AK1 and AK2 have been purified from the adductor muscle of the scallop, Pecten maximus. AK2 was retained on a DEAE-cellulose column at pH 7.5, but AK1 was not. 2. Both forms were monomeric (mol. wt. approximately 42,000) and showed the same pH optimum (7.5-8.0) in the direction of phosphoarginine synthesis. 3. AK1 had slower electrophoretic mobility at pH 8.3 towards the anode, higher lysine content, lower glutamate content, lower Km for L-arginine and higher Km for Mg(2+)-ATP than AK2. Unlike AK1, AK2 was strongly inhibited at high concentrations of Mg(2+)-ATP. 4. Both molecular forms cross-reacted with antisera raised against native as well as performic acid-oxidized lobster muscle arginine kinase. However, AK1 showed a greater affinity than AK2 to anti-lobster arginine kinase antibodies, particularly to those raised against the native enzyme.
authors.affiliation: UPR 8402 Centre de Recherches de Biochimie Macromoléculaire (CNRS), U 249 INSERM, Université de Montpellier I, France.
authors.forename: S R
authors.initials: SR
authors.lastname: Reddy
authors.forename: C
authors.initials: C
authors.lastname: Roustan
authors.forename: Y
authors.initials: Y
authors.lastname: Benyamin
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001122:Arginine Kinase / Q000302:isolation & purification* / Q000378:metabolism; D015153:Blotting, Western; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008974:Mollusca / Q000201:enzymology*; D009132:Muscles / Q000201:enzymology*; D008121:Nephropidae
chemical_list: D000596:Amino Acids; D007527:Isoenzymes; D001122:Arginine Kinase