Electron microscopic and biochemical evidence that proline-β-naphthylamidase is composed of three identical subunits |
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Authors: | T Takahashi M Nishigai A Ikai K Takahashi |
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Affiliation: | Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan. |
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Abstract: | Electron microscopy of pig intestinal proline-β-naphthyltamidase revealed that the enzyme is composed of 3 subunits, which are assembled in a trifoliolate shape, At pH 4.5 and 4°C, the enzyme dissociates reversibly into active subunits in 4h. Dissociation also occurs at higher pHs when the enyzme 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. |
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Keywords: | Proline-β-naphthylamidase Electron micrograph Trimer protein, Subunit dissociation |
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