The 60‐kDa precursor to the dithiothreitol‐sensitive tetrameric protease of spinach thylakoids: structural similarities between the protease and polyphenol oxidase

FEBS Letters

Kuwabara, Tomohiko¹ 

[1] Institute of Biological Sciences, University of Tsukuba, Tsukuba, Ibaraki 305, Japan

关键词: Dithiothreitol-sensitive tetrameric protease;    Metallo-protease;    Photosystem II;    Polyphenol oxidase;    Spinach thylakoid;    Buffer A;    20 mM sodium phosphate (pH 6.5)/0.3 M NaCl;    DTT;    dithiothreitol;    PPO;    polyphenol oxidase;    PS;    photosystem;   

DOI  :  10.1016/0014-5793(95)00911-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The 60-kDa precursor to the 39-kDa dithiothreitolsensitive protease was purified from photosystem II membranes of spinach. When partially purified 60-kDa protein was stored at 4°C, the protein was degraded to fragments of 39 and 21 kDa. The 39-kDa fragment was suggested to be identical to the 39-kDa protease from effects of dithiothreitol on these polypeptides. The N-terminal amino acid sequences of the 60-kDa protein and the 39-kDa protease were the same, APILPDVEK-, suggesting that the latter was derived from the N-terminal portion of the former. Immunostaining with polyclonal antibodies against the 60-kDa protein indicated that the 60-kDa protein represents the species that occurs in the native thylakoids. These and other structural properties suggest that the protein might be identical to polyphenol oxidase.

【 授权许可】

Unknown