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Electron microscopic and biochemical evidence that proline‐β‐naphthylamidase is composed of three identical subunits
Author(s) -
Takahashi Takayuki,
Nishigai Masaaki,
Ikai Atsushi,
Takahashi Kenji
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80316-u
Subject(s) - proline , chemistry , protein subunit , biochemistry , biophysics , crystallography , stereochemistry , amino acid , biology , gene
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.