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J. Biochem, 1984, Vol. 96, No. 4 1125-1131
© 1984 Japanese Biochemical Society

research-article

Mammalian Signal Peptidase: Partial Purification and General Characterization of the Signal Peptidase from Microsomal Membranes of Porcine Pancreas1

Yukio FUJIMOTO, Yasuhiro WATANABE, Masahide UCHIDA and Masakazu OZAKI

Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences Katsuraoka-cho, Otaru, Hokkaido 047–02

Signal peptidase has been enriched extensively from microsomal membranes of porcine pancreas. Microsomal membranes were washed with 1 M KCl and Brij 35, and then solubilized with 1% Nonidet P-40. The solubilized signal peptidase was purified by DEAE-cellulose chromatography and Sepharose CL-6B filtration. Cleavage of pre-human placental lactogen with the partially purified enzyme gave the mature form, whose NH2-terminus was identified as valine. The signal peptidase is heat-labile and approximately 90% of the enzymatic activity was lost at 60°C within 1 min. The pH optimum of the activity was 7 to 8. Chymostatin and o-phenanthroline at concentrations of 2.5 mM inhibited the signal peptidase activity by 62% and 30%, respectively.

1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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