Vanag V K, Kuznetsov A N, Piruzian L A
Biofizika. 1983 Jan-Feb;28(1):18-23.
The rate constants of H2O2 decomposition equal to 0.45 X 10(7) M-1S-1 per hem and Michaelis constants higher than 0.3 M were found by gas volume meter and spectrophotometer methods for purified preparations of catalase from bovine liver. Unlike the results obtained earlier the magnetic field with induction 0.65 T and 0.012 T does not affect the constant rate within 3%. It was found with the substrate concentration less than 0.01 M when the classical catalase mechanism was observed and with higher concentration of the substrate up to 0.7 M when the catalase inhibition by H2O2 played an important role.
通过气体体积计和分光光度计法，针对从牛肝中纯化得到的过氧化氢酶制剂，发现其H2O2分解速率常数为每血红素0.45×10(7) M-1S-1，米氏常数高于0.3 M。与早期获得的结果不同，感应强度为0.65 T和0.012 T的磁场在3%范围内不影响恒定速率。当底物浓度小于0.01 M时观察到经典的过氧化氢酶机制，而当底物浓度高达0.7 M时，H2O2对过氧化氢酶的抑制作用起重要作用。
