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Purification and Chemical Properties of Two 1,3;1,4-β-Glucan Endohydrolases from Germinating Barley.
- Source :
- European Journal of Biochemistry; 1/15/82, Vol. 121 Issue 3, p663-669, 7p
- Publication Year :
- 1982
-
Abstract
- Two 1,3; 1,4-β-glucan endohydrolases have been purified from extracts of germinating barley by ammonium sulphate precipitation, ion-exchange and gel filtration chromatography. Both enzymes are monomeric, basic proteins. Enzyme I has a molecular weight of 28000 and an isoelectric point of 8.5, while enzyme II has a molecular weight of 33000 and an isoelectric point greater than 10. Enzyme II is a glycoprotein containing 3.6% carbohydrate, of which three residues are probable N-acetylglucosamine, but enzyme I contains only traces of associated carbohydrate. The amino acid compositions of the two 1,3; 1,4-β-glucan endohydrolases are similar and the cross-reactivity of antibodies raised against the purified enzymes suggests that they share common antigenic determinants. [ABSTRACT FROM AUTHOR]
- Subjects :
- ENZYMES
GERMINATION
BARLEY
PROTEINS
MOLECULAR weights
AMINO acids
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 121
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 15801521
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1982.tb05837.x