Isolation of a pure dextranase from Penicillium funiculosum.
- 1 September 1970
- journal article
- Vol. 20 (3) , 421-6
Abstract
A dextranase, produced by Penicillium funiculosum, was purified 1,000-fold to yield the enzyme which was demonstrated by gel electrophoresis and electrofocusing to be a homogeneous protein. The purification method included acetone partition, ammonium sulfate fractionation, gel filtration, iron defecation and precipitation, and diethylaminoethyl-cellulose chromatography. The pure enzyme was also obtained by preparative gel electrophoresis. Gel-permeation chromatography indicates a molecular weight of 41,000. An isoelectric pH of 4.6 was established by electrofocusing. A 1-mg amount of the enzyme hydrolyzes a dextran substrate to yield 27,000 isomaltose reducing units in 2 hr.This publication has 8 references indexed in Scilit:
- Heterogeneity of Presumably Homogeneous Protein PreparationsScience, 1969
- A versatile system for preparative electrophoresis in acrylamide gelAnalytical Biochemistry, 1969
- A technique for the crystallization of proteinsAnalytical Biochemistry, 1968
- Enzymatic removal of artificial plaquesArchives of Oral Biology, 1968
- Isoelectric Fractionation, Analysis, and Characterization of Ampholytes in Natural pH Gradients. IV. Further Studies on the Resolving Power in Connection with Separation of Myoglobins.Acta Chemica Scandinavica, 1966
- DISC ELECTROPHORESIS‐I BACKGROUND AND THEORY*Annals of the New York Academy of Sciences, 1964
- NON‐IONIC SEPARATIONS WITH ION EXCHANGE RESINSAnnals of the New York Academy of Sciences, 1953