[Isolation of the heterodimer of porcine MB creatine phosphokinase and the study of its binding with polyclonal antibodies].
Heterodimers of porcine creatine phosphokinase were obtained from dissociated MM and BB isoenzymes and investigated in the enzyme-linked immunosorbent assay. It has been shown that peroxidase conjugates of rabbit polyclonal antibodies against porcine enzymes have low affinity in the sandwich reaction.
D000818:Animals; D000915:Antibody Affinity; D001666:Binding Sites, Antibody; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D003402:Creatine Kinase / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D007114:Immunization; D005779:Immunodiffusion; D007527:Isoenzymes; D011817:Rabbits; D013552:Swine
D007527:Isoenzymes; D003402:Creatine Kinase
Poluchenie geterodimera MB-kreatinfosfokinazy svin'y i issledovanie ego sviazyvaniia s poliklonal'nymi antitelami.