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J. Biochem, 1997, Vol. 121, No. 4 642-647
© 1997 Japanese Biochemical Society

research-article

Release of a Newly-Identified Cysteine Protease, Tetrain, from Tetrahymena into Culture Medium during the Cell Growth1

Kazu-Michi Suzuki*, Natsumi Hosoya{dagger}, Tadao Takahashi*, Toshikazu Kosaka* and Hiroshi Hosoya*,2

*Department of Biological Science, Faculty of Science, Hiroshima University Higashi-Hiroshima, Hiroshima 739
{dagger}School of Social Information Studies, Otsuma Women's University Karakida, Tamo, Tokyo 206

2To whom correspondence should be addressed. Tel: +81-824-24-7443, Fax: +81-0824-24-0734, E-mail: hhosoya{at}sci.hiroshima-u.ac.jp

Protease activity in the culture medium of Tetrahymena pyriformis markedly increased during the growth of the ciliate. The protease activity in the culture medium was purified by sequential column chromatographies. The purified protease had an apparent molecular mass of 28 kDa. N-terminal amino acid sequencing analysis suggested that the protease is a mature form of cysteine protease. Requirements of free sulfhydryl groups for activity and sensitivity to N-tosyl-L-phenylalanine chloromethyl ketone and N{alpha}-p-tosyl-L-lysine chloromethyl ketone also indicated that the protease is a member of the papain family of cysteine proteases. The protease was designated as tetrain. Immunoblotting analyses showed that tetrain was present in higher amount in the culture medium in the stationary phase than in the logarithmic phase. Tetrain has high activities at neutral to alkaline pH values. This suggests that tetrain has functional roles in the culture medium in the stationary phase, because the pH of the culture medium became alkaline with the progress of Tetrahymena growth.

1This work was supported in part by grants for Scientific Research from The Narishige Zoological Science Award, The Uehara Memorial Foundation, and The Naito Foundation.


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