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. 2008 May 16;4(5):e1000062. doi: 10.1371/journal.ppat.1000062

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Tsuji et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Ten micrograms of native spectrin were incubated with longipain for 6 h. The hydrolysis pattern was analyzed by 6% SDS-PAGE and proteins were transferred to a nitrocellulose membrane and reacted with rabbit anti-human spectrin serum. (A) Dose-dependant hydrolysis of rabbit erythrocyte spectrin. Spectrin alpha and beta are indicated by arrowheads. The hydrolytic fragments are indicated by arrows. (B) Effect of pH on the hydrolysis of spectrin. (C) Effect of temperature on the hydrolysis of spectrin. The results demonstrated that longipain hydrolyzed rabbit erythrocyte spectrin over a wide range of pH and temperature.