| DOI | Resolve DOI: https://doi.org/10.1139/o54-003 |
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| Author | Search for: Wetter, L. R.1 |
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| Affiliation | - National Research Council of Canada. Prairie Regional Laboratory
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| Format | Text, Article |
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| Abstract | Moving-boundary electrophoresis indicated that a protease concentrate obtained from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) was made up of a number of proteins. Filter-paper electrophoresis demonstrated that two of the proteins were capable of hydrolyzing denatured hemoglobin. One active component had a negative mobility, the other a positive mobility in phosphate buffer pH 6.8, ionic strength 0.1. Because of the difference in electrical properties it was possible to separate the two active components by zone electrophoresis. Though yields were low when filter paper was employed, the use of potato starch as the supporting medium resulted in excellent recoveries. |
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| Publication date | 1954-01-01 |
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| Publisher | Canadian Science Publisher |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| Identifier | NRCC-3129 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 0a7a1c4f-1811-4251-958f-0a1ab0812b06 |
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| Record created | 2023-09-05 |
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| Record modified | 2023-09-05 |
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