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Purification and characterization of furin, a Kex2-like processing endoprotease, produced in Chinese hamster ovary cells. by K Hatsuzawa; M Nagahama; S Takahashi; K Takada; K Murakami; K Nakayama is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Furin, a mammalian homolog of the yeast Kex2 protease, is associated with Golgi membranes and is involved in cleavage of precursor proteins at sites marked by the Arg-X-Lys/Arg-Arg (RXK/RR) motif. We have recently shown that a furin mutant lacking the transmembrane domain can be secreted from cDNA-transfected cells with proteolytic activity for the fluorogenic peptide t-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin-7- amide. In this study, we purified and characterized the recombinant furin from the conditioned medium of these cells. Furin was purified as a mixture of 83- and 81-kDa forms and a 96-kDa form. The differences in molecular mass were not due to differences in molecular mass were not due to differences in glycosylation. Moreover, all forms had the same NH2-terminal sequence beginning at the residue after the Arg-Ala-Lys-Arg sequence. These data suggest that the three different forms may be produced by differential COOH-terminal processing of a furin molecule and that mature furin may be autocatalytically produced. Both enzyme preparations showed a pH optimum at 7.0, required Ca2+ for the activity, and showed essentially the same inhibitor profile. These properties rese

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Author

K Hatsuzawa; M Nagahama; S Takahashi; K Takada; K Murakami; K Nakayama

Publisher

Elsevier BV

Published

1992

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)