ISSN:
1432-072X
Schlagwort(e):
Acinetobacter calcoaceticus
;
Periplasm
;
Insulin
;
cleaving proteinase
;
Protease Pi
;
Protease III
;
Substrate specificity
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
Notizen:
Abstract 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 108000 (gel filtration) or 112000 (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).
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00249104
Permalink
