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- W2411288045 abstract "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." @default.
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- W2411288045 date "1980-11-01" @default.
- W2411288045 modified "2023-09-23" @default.
- W2411288045 title "[Metalloproteinase from Bacillus subtilis: - intracellular and extracellular enzymes]." @default.
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