[Retention of specific activity of muscle aldolase after its immobilization on odigos and odifil (ethylsulfo-activated agarose)].
The effect of the number of active groups of new affinity supports--odigose and odifil (ethylsulfo-activated agarose) on the retention of the specific activity of muscle aldolase was investigated. The active center of the enzyme includes lysine able to react with activated supports. The aldolase completely retained the specific activity after immobilization on the abovementioned relatively high-substituted supports, on which other enzymes, e.g. phosphorylase B, NAD-kinase from pigeon heart, were partially or completely inactivated. The aldolase was inactivated when being immobilized on more substituted supports. The enzyme specific activity completely retained if the high substituted supports were preliminary incubated at 37 degrees to destroy some diazo-groups.
Kuzovleva
O V
OV
Bedishcheva
I B
IB
Truus
K E
KE
D000818:Animals; D004791:Enzyme Inhibitors; D004800:Enzymes, Immobilized; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits; D012685:Sepharose / Q000031:analogs & derivatives
D004791:Enzyme Inhibitors; D004800:Enzymes, Immobilized; D012685:Sepharose; D005634:Fructose-Bisphosphate Aldolase
Sokhranenie udel'noĭ aktivnosti myshechnoĭ al'dolazy posle ee immobilizatsii na odigoze i odifile (étilsul'foaktiviravannoĭ agaroze).