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- W2024811245 abstract "Abstract Two proteinases of Aspergillus niger, one of pH optimum 3·4, the other of pH optimum 7·4, were purified 840- and 740-fold by (NH4)2SO4 precipitation Sephadex G-100, G-150 and G-200 gel chromatography. Both proteinases were assayed using [3H]acetyl hemoglobin as substrate. The purified pH 3·4 proteinase had two bands on sodium dodecylsulfate polyacrylamide gel electrophoresis, while the purified pHH 7·4 proteinase gave one band when stained for protein; none of the purified material stained for glycoprotein. The purified pH 3·4 proteinase had molecular weights of 49 000 and 56 000, pI of 4.1 and 4.5 and a Km of 1·10−5 M. This acid proteinase showed no cofactor requirements, was inhibited 51% by o.1 M HgCl2, and was relatively inactive against synthetic substrates of low molecular weight. Analysis of the products of digestion of the [3H]acetyl hemoglobin after 1 h digestion with this enzyme showed that 71% of the product consisted of peptides of molecular weights less than 4000. The purified pH 7·4 proteinase had a molecular weight of 68 000, pI of 6.2, and a Km of 5·10−5 M. This neutral proteinase showed no cofactor requirements, was severely inhibited by HgCl2 and diisopropylphosphofluoridate and was also relatively inactive against low molecular weight synthetic substrates. Analysis of the products of digestion with this neutral proteinase showed that 66% of the product consisted of peptides of molecular weight less than 4000." @default.
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- W2024811245 date "1973-02-01" @default.
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- W2024811245 title "Protein catabolism. II. Identification of neutral and acidic proteolytic enzymes in Aspergillus niger" @default.
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- W2024811245 doi "https://doi.org/10.1016/0005-2744(73)90354-9" @default.
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