On the mechanism of metal activation of deoxyribonuclease I

作者: John S. Wiberg

DOI: 10.1016/0003-9861(58)90280-7

关键词: Ethylenediaminetetraacetic acidIonic strengthDissociation constantMetal saltsMetalQualitative inorganic analysisDeoxyribonuclease IChemistryMaximum rateInorganic chemistryBiophysicsBiochemistryMolecular biology

摘要: Abstract 1. The activation of deoxyribonucleasc I (DNase I) by Mg ++ , Mn and Ca has been studied at 27 °C., an ionic strength 0.15, a pH 7.5 - 7.2. Alone, the metals rank us activators in order > ⪢ . 2. Activity presence or shown to require formation “metallosubstrate.” 3. In study pairs these metals, was found be potent Synergist Mg-activated reaction, increasing maximum rate more than threefold, give comparable that given alone. Several possible explanations are suggested. 4. A rapid method is described for standardizing solutions large number bivalent metal salts. 5. pitfalls DNase assay methods discussed modifications 6. inhibition citrate deprecated; ethylenediaminetetraacetic acid suggested replace citrate. 7. dissociation constant determined 1.90 ± 0.13 × 10 −4 using ion-exchange radioisotope method.

参考文章(64)
V. Allfrey, A. E. Mirsky, Some aspects of the desoxyribonuclease activities of animal tissues. The Journal of General Physiology. ,vol. 36, pp. 227- 241 ,(1952) , 10.1085/JGP.36.2.227
Lew Cunningham, M. Laskowski, Presence of two different desoxyribonucleodepolymerases in veal kidney Biochimica et Biophysica Acta. ,vol. 11, pp. 590- 591 ,(1953) , 10.1016/0006-3002(53)90104-8
E.A. Robbins, M.P. Stulberg, P.D. Boyer, The magnesium activation of pyrophosphatase. Archives of Biochemistry and Biophysics. ,vol. 54, pp. 215- 222 ,(1955) , 10.1016/0003-9861(55)90024-2
Connell Marsh, Walter Militzer, Thermal enzymes. VIII. Properties of a heat-stable inorganic pyrophosphatase Archives of Biochemistry and Biophysics. ,vol. 60, pp. 439- 451 ,(1956) , 10.1016/0003-9861(56)90449-0
Toru Miyaji, Jesse P. Greenstein, Cation activation of desoxyribonuclease. Archives of Biochemistry and Biophysics. ,vol. 32, pp. 414- 423 ,(1951) , 10.1016/0003-9861(51)90291-3
Thomas R. Koszalka, Kurt Schreier, Kurt I. Altman, The separation of two urinary desoxyribonucleases. Biochimica et Biophysica Acta. ,vol. 15, pp. 194- 197 ,(1954) , 10.1016/0006-3002(54)90059-1
S. Dagley, E.A. Dawes, Citridesmolase: Its properties and mode of action Biochimica et Biophysica Acta. ,vol. 17, pp. 177- 184 ,(1955) , 10.1016/0006-3002(55)90348-6
B.R. Rabin, E.M. Crook, The activation of enzymes by metal ions. Biochimica et Biophysica Acta. ,vol. 19, pp. 550- 551 ,(1956) , 10.1016/0006-3002(56)90482-6
Edwin G. Krebs, Edmond H. Fischer, The phosphorylase b to a converting enzyme of rabbit skeletal muscle. Biochimica et Biophysica Acta. ,vol. 20, pp. 150- 157 ,(1956) , 10.1016/0006-3002(56)90273-6
Robert Hays, W.D. McElroy, Jane Coulombre, Properties of firefly pyrophosphatase. Archives of Biochemistry and Biophysics. ,vol. 32, pp. 207- 215 ,(1951) , 10.1016/0003-9861(51)90255-X