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Comparison of Alkaline Proteinase from Hyperproductive
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- NASUNO Seiichi
- Noda Institute for Scientific Research
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- OHARA Tadahiko
- Noda Institute for Scientific Research
Bibliographic Information
- Other Title
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- Mutants and Parent Strain of <i>Aspergillus sojae</i>
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Description
Physico-chemical properties of alkaline proteinase from the parent strain were compared with those from hyperproductive mutants of Aspergillus sojae. All the results on behavior of enzyme protein to ion exchange resin and celluloses, gel filtration, ultracentrifugal sedi-mentation, disc electrophoresis and isoelectrofocusing on polyacrylamide gel column, specific activity, substrate specificity, and kinetic constants provided evidence in favor of the con-clusion that the parent and mutant strains produced the chemically identical enzymes and that superactivity of alkaline proteinase in culture extracts or filtrates of mutant strains was not attributed to alteration of catalytic property of the enzyme, but to hyperproduction of the identical enzyme resulting from the genetic change in the regulatory mechanism of enzyme synthesis.
Journal
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 35 (6), 836-842, 1971
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390282681448793600
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- NII Article ID
- 130003523695
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- COI
- 1:CAS:528:DyaE3MXkslars7Y%3D
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- ISSN
- 18811280
- 00021369
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- Text Lang
- en
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed