Effects of Trypsin Treatment on the Photochemical Activity and Polypeptide Composition of the P700-Chlorophyll a Protein Complex(Biological Chemistry)

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The P700-chlorophyll a protein complex purified from spinach consists of polypeptides of molecular mass 60〜65, 23, 20, 17, 14, and 12kD. Proteolysis of the complex with trypsin for 24hr altered neither the photochemical activity of P700-chlorohyll a protein complex nor the characteristic effects of cations and pH on the electron transfer from plastocyanin to photooxidized P700. However, it was found that the trypsin-treated complex was photochemically inactive in the presence of 1% (v/v) Triton X-100, although 1% (v/v) Triton X-100 had no effect on the photochemical activity of the native complex. Upon lowering the concentration of Triton X-100 by dialysis, the digested complex regained the photochemical activity of P700. The results of SDS-polyacrylamide gel electrophoresis showed that proteolysis of the complex with trypsin for 24hr results in extensive degradation of polypeptides associated with this complex into small polypeptide fragments (M.W. <__- 14.000). Isolated reaction center protein (60〜65 kD polypeptide) was also treated with trypsin and we observed quite similar effects of trypsin treatment. All these data suggest that the structure of either trypsin digested P700-chlorophyll a protein complex or the reaction center protein required for its photochemical activity can be maintained through strong hydrophobic interactions among the nicked subunit polypeptides.
社団法人日本農芸化学会の論文
1986-05-23