Abstract
THE recent development in this laboratory of methods for producing acid proteinase of Aspergillus saitoi (EC, 3.4.4.17, aspergillopeptidase A) from culture filtrate has made available sufficient material for a correlative study of its enzymatic properties1,2. The optimal pH for milk casein digestion is in the pH range of 2.5–3.0 and the proteinase is fairly stable over the pH range of 2.5–6.0 (ref. 3). Aspergillopeptidase A is capable of activating trypsinogen and chymotrypsinogen A at pH 4.5 (ref. 4). The further purification method for separating acid proteinase has been improved by chromatographic procedures with the use of ion exchange materials, ‘Duolite CS-101’, DEAE-cellulose and ‘SE-Sephadex’5. The purified aspergillopeptidase A appears to be homogeneous on free boundary electrophoresis over a pH range of 2.0–10.0 and on ultracentrifugation at pH 4.1. The iso-electric point has been found to be at pH 3.65 in Sørensen's citrate buffer. In the investigation reported here, the molecular weight of aspergillopeptidase A was found to be 34,900 from sedimentation and viscosity, according to Scheraga–Mandel-kern's formula6,7, and was also determined to be 34,200 according to Yphantis's treatment8.
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References
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ICHISHIMA, E., YOSHIDA, F. Molecular Weight of Acid Proteinase of Aspergillus saitoi. Nature 207, 525–526 (1965). https://doi.org/10.1038/207525a0
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DOI: https://doi.org/10.1038/207525a0
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