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Electron microscopic and biochemical evidence that proline-beta-naphthylamidase is composed of three identical
T Takahashi1, M Nishigai, A Ikai
1Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
FEBS Letters
|March 25, 1991
Abstract:
Electron microscopy of pig intestinal proline-beta-naphthylamidase revealed that the enzyme is composed of 3 subunits, which are assembled in a trifoliolate shape. At pH 4.5 and 4 degrees C, the enzyme dissociates reversibly into active subunits in 4 h. Dissociation also occurs at higher pHs when the enzyme concentration is very low. The activity per mg protein of the native, trimeric enzyme is about 2.5-fold higher than that of the dissociated enzyme.