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- W2009412488 abstract "A procedure is described which results in a 750-fold purification of acid deoxyribonuclease (deoxyribonucleate 3′-oligonucleotidohydrolase, EC 3.1.4.6; deoxyribonuclease II) from cultured HeLa S3 cells. Methods are also described for the additional purification of a commercially available, partially purified calf-spleen acid deoxyribonuclease (Worthington Biochemicals) Treatment of either the HeLa or calf-spleen acid deoxyribonuclease with 2-mercaptoethanol resulted in the production of at least two modified, enzymatically active species of acid deoxyribonuclease which could be clearly resolved from the native enzyme molecules by chromatography on carboxymethyl-cellulose columns. The sedimentation constant of each of these mercaptoethanol-elicited species was compared with that of the native enzyme and found to be slightly lower All species of the enzyme (native or modified) were capable of degrading native DNA by ‘single hit’ kinetics Heat-denatured DNA was found to be an inhibitor of native DNA hydrolysis by acid deoxyribonuclease. Low amounts of heat-denatured DNA acted as a non-competitive inhibitor of native DNA degradation by acid deoxyribonuclease while higher amounts of denatured DNA acted as a competitive inhibitor of native DNA hydrolysis. In both of the mercaptoethanol-elicited modified species of acid deoxy-ribonuclease, low and high amounts of denatured DNA acted as competitive inhibitors of native DNA hydrolysis In the case of the merceptoethanol-elicited modified enzyme species, possible allosteric effects were observed inasmuch as the enzyme in combination with denatured DNA was activated in a sigmoidal fashion by the addition of increasing amounts of native DNA substrate A ‘two active site’ model is presented for acid deoxyribonuclease and discussed in terms of the present kinetic data" @default.
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- W2009412488 date "1967-03-01" @default.
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- W2009412488 title "Purification of acid deoxyribonuclease from HeLa cells. Inhibition kinetics of native and modified forms of the HeLa and calf-spleen enzymes" @default.
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- W2009412488 doi "https://doi.org/10.1016/0005-2744(67)90161-1" @default.
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