Metalloproteinase from Bacillus subtilis: - "intracellular" and extracellular enzymes
Shaginian, K.A.; Izotova, L.S.; Iomantac, I.V.; Strongin, A.I.; Stepanov, V.M.
Biokhimiia 45(11): 2083-2095
1980
ISSN/ISBN: 0320-9725 PMID: 6786372 Document Number: 160135
"Intracellular" metalloproteinase was purified to homogeneity from Bacillus subtilis 103 crude cell extract, using affinity chromatography on bacitracin-Sepharose 4B. The degree of purification and the yield of the enzyme were about 260-fold and 3%, respectively. In its physico-chemical properties and the amino acid composition the enzyme is very similar, if not identical, to the extracellular metalloproteinase isolated from the culture filtrate of the same strain. Extracellular metalloproteinase-deficient mutant strain Bacillus subtilis SMY-512 does not produce the "intracellular" enzyme either. THe activity of "intracellular" metalloproteinase in the periplasmic space of the cells is about 70% of that in the cytoplasm, thus being indicative of a rather regular distribution of the enzyme throughout the cell compartment.