SharePURIFICATION, CRYSTALLIZATION AND SOME PROPERTIES OF LOW-TEMPERATURE-ACTIVE INTRACELLULAR PROTEINASE FROM STREPTOCOCCUS LACTIS.
Author(s) : AKUZAWA R., YOKOYAMA K.
Type of article: Article
Summary
DESCRIPTION OF PURIFICATION AND CRYSTALLIZATION PROCESSES. MEASUREMENT OF ENZYMIC ACTIVITY. ELECTROPHORETIC PROFILE. CRYSTALLINE PROTEINASE HAS A MAXIMUM ACTIVITY AT 279 K (6 DEG C) AT A PH OF 5.5. (Bibliogr. int. CDIUPA-CNRS, FR., 83-210-1704.
Details
- Original title: PURIFICATION, CRYSTALLIZATION AND SOME PROPERTIES OF LOW-TEMPERATURE-ACTIVE INTRACELLULAR PROTEINASE FROM STREPTOCOCCUS LACTIS.
- Record ID : 1984-0781
- Languages: English
- Source: Nippon Chikusan Gakkai-Ho - vol. 53 - n. 12
- Publication date: 1982
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Indexing
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EFFECTS OF CRYOPROTECTANTS ON ENZYME STRUCTURE.
- Author(s) : FINK A. L.
- Date : 1986
- Languages : English
- Source: Cryobiology - vol. 23 - n. 1
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- Date : 1986
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- Source: Cryobiology - vol. 23 - n. 1
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