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Oligomerization of the cytotoxin alpha-sarcin associated with phospholipid membranes.

作者信息

Oñaderra M, Mancheño J M, Lacadena J, de los Rios V, Martínez del Pozo A, Gavilanes J G

机构信息

Departamento de Bioquímica y Biología Molecular, Facultad de Química, Universidad Complutense, Madrid, Spain.

出版信息

Mol Membr Biol. 1998 Jul-Sep;15(3):141-4. doi: 10.3109/09687689809074525.

Abstract

alpha-Sarcin is a cytotoxic protein that specifically inactivates ribosomes. The protein translocates across phospholipid membranes. Oligomerization of the protein occurs upon interaction with membranes. Chemically cross-linked protein oligomers have been obtained by treatment of protein-vesicle complexes with the membrane impermeant reagent bis-(sulfosuccinimidyl) suberate. These structures are only obtained in the presence of acidic lipid vesicles composed of either natural or synthetic phospholipids. Such oligomers are not produced in concentrated protein solutions in the absence of vesicles. The formation of the chemically stabilized oligomers is saturated at the same lipid to protein molar ratio as all the perturbations caused by alpha-sarcin on lipid vesicles. Results are discussed in terms of the involvement of oligomer formation on protein translocation across membranes.

摘要

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