Affinity purification, crystallization, and amino acid analysis of hog kidney mutarotase type II.
- 1 January 1982
- journal article
- research article
- Published by Pharmaceutical Society of Japan in CHEMICAL & PHARMACEUTICAL BULLETIN
- Vol. 30 (8) , 2880-2884
- https://doi.org/10.1248/cpb.30.2880
Abstract
Hog kidney mutarotase type II was purified to polyacrylamide disc gel electrophoretic homogeneity by a 5-step procedure including affinity chromatgraphy with phloretin-linked agarose. The purified enzyme was crystallized, and the crystals were subjected to amino acid analysis. The amino acid composition of the enzyme was similar to that of bovine kidney mutarotase, except for marked differences in the contents of phenylalanine and methionine.This publication has 8 references indexed in Scilit:
- Comparative immunological studies of mutarotases from mammals.CHEMICAL & PHARMACEUTICAL BULLETIN, 1981
- Purification and properties of hog kidney mutarotase.CHEMICAL & PHARMACEUTICAL BULLETIN, 1981
- Amination and Subsequent Derivatization of Epoxy-ActivatedThe Journal of Biochemistry, 1980
- Activation of Sepharose with Epichiorohydrin and Subsequent Immobilization of Ligand for Affinity AdsorbentThe Journal of Biochemistry, 1979
- Comparison of non-biospecific effects in immunoaffinity chromatography using cyanogen bromide and bifunctional oxirane as immobilising agentsJournal of Chromatography A, 1977
- Multiple forms of rat kidney mutarotase.CHEMICAL & PHARMACEUTICAL BULLETIN, 1976
- [37] Reaction of protein sulfhydryl groups with Ellman's reagentPublished by Elsevier ,1972
- Kinetics and Distribution of Mutarotases and Their Relation to Sugar TransportJournal of Biological Chemistry, 1964