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Can I read Purification of a periplasmic insulin-cleaving proteinase from Acinetobacter calcoaceticus on EtoBox?
Purification of a periplasmic insulin-cleaving proteinase from Acinetobacter calcoaceticus by B. Fricke; H. Aurich is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Purification of a periplasmic insulin-cleaving proteinase from Acinetobacter calcoaceticus about?
Cells of Acinetobacter calcoaceticus contain a constitutive periplasmic metalloproteinase showing similar properties as the periplasmic metalloproteinase of Escherichia coli. The periplasmic proteinase of A. calcoaceticus was purified, starting from periplasm, by ammonium sulfate precipitation, hydrophobic interaction chromatography and chromatofocusing up to the homogeneity of the enzyme in SDS-electrophoresis with a yield of 6.7% and a purification factor of 417. The enzyme has a molecular mass of 108,000 (gel filtration) or 112,000 (native electrophoresis), and consists of four identical subunits with a molecular mass of 27,000 (SDS-electrophoresis). The purified enzyme degrades preferentially polypeptides such as glucagon and insulin. Larger proteins are accepted as substrates to a considerably lower extent. All tested synthetic substrates with trypsin, chymotrypsin, elastase and thermolysin specificity were not cleaved. Therefore, the described enzyme was designated "insulin-cleaving proteinase" (ICP).
Who reads Purification of a periplasmic insulin-cleaving proteinase from Acinetobacter calcoaceticus?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- B. Fricke; H. Aurich
- Publisher
- Springer; Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC; Archie Comics (ISSN 0302-8933)
- Published
- 1992
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)