European Journal of Biochemistry · 1972 · 18 citations · 16 references
Life SciencesBiochemistryEndocrinologyEnzymologyMetabolismSteroid BiochemistryEnzyme CharacterizationEnzyme FunctionEnzyme IsolationEnzyme KineticsEnzyme PurificationEnzyme Activity KineticsEnzyme Reaction KineticsEnzyme SolubilizationMicrosomal Enzyme ActivityPh Effects On Enzyme ActivityPh OptimaSolubilizationSteroidogenic Enzyme Kinetics
“Solubilization” of a beef adrenal microsomal enzyme: 3‐oxosteroid Δ 5 ‐Δ 4 ‐isomerase has been obtained by high concentrations of divalent cation (0.5–2 M CaCl 2 ). A study of the Solubilization yield as a function of ion concentration and pH has shown that optimum yield is obtained with 1 M CaCl 2 near pH 7. After elimination of calcium from the “soluble” enzyme, precipitation occurs and enzymatic activity is irreversibly lost in both precipitate and supernatant. The values of the kinetic parameters determined at pH 8.5 and 35°C are: V = 410 and 920 nmol · min −1 · mg −1 and K m = 36 and 11 μM for 5‐androstene‐3,17‐dione and 5‐pregnene‐3,20‐dione respectively. Our results suggest the existence of only one C 19 and C 21 3‐oxosteroid isomerase in the beef adrenal glands.
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The Theory of Emulsification, V
Wilder D. Bancroft · The Journal of Physical Chemistry · 1913 · 419 citations
G. H. A. Clowes · The Journal of Physical Chemistry · 1916 · 119 citations
T. Gulik‐Krzywicki, Emanuel Shechter, Motohiro Iwatsubo et al. · Biochimica et Biophysica Acta (BBA) - Biomembranes · 1970 · 81 citations
Ronald W. McCune, Sidney Roberts, Peggy L. Young · Journal of Biological Chemistry · 1970 · 63 citations · Full text