The β-galactosidase system of Neurospora crassa: I. Purification and properties of the pH 4.2 enzyme

Extracts of Neurospora crassa contain a β-galactosidase with a pH optimum of 7.5 and a β-galactosidase with a pH optimum of 4.2. The pH 4.2 enzyme was purified by ammonium sulfate precipitation and cation-exchange chromatography. The physical properties of the purified enzyme were similar to those o...

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Bibliographic Details
Published inArchives of biochemistry and biophysics Vol. 138; no. 2; pp. 408 - 411
Main Authors Johnson, H.N., DeBusk, A.Gib
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.06.1970
Subjects
Amino Acids - analysis
Arginine - analysis
Chemical Precipitation
Chromatography, Ion Exchange
Electrophoresis
Galactosidases - isolation & purification
Hot Temperature
Hydrogen-Ion Concentration
Methods
Neurospora - enzymology
Protein Denaturation
Quaternary Ammonium Compounds
Sulfates
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Summary:Extracts of Neurospora crassa contain a β-galactosidase with a pH optimum of 7.5 and a β-galactosidase with a pH optimum of 4.2. The pH 4.2 enzyme was purified by ammonium sulfate precipitation and cation-exchange chromatography. The physical properties of the purified enzyme were similar to those of the nonpurified enzyme as reported previously, but arginine was absent from the former.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(70)90363-2