Identification of four starch‐branching enzymes in barley endosperm: partial purification of forms I, IIa and IIb
- 1 October 1997
- journal article
- Published by Wiley in New Phytologist
- Vol. 137 (2), 215-222
- https://doi.org/10.1046/j.1469-8137.1997.00796.x
Abstract
Developing caryopses of barley (Hardeum vulgare L. ev. Golf) were monitored for starch-branching enzyme activity for 1 month after anthesis. Homogenized caryopses from grains with the highest specific activity were used as starting material for purification of branching enzyme by FPLC chromatography. Several branching enzyme activity fractions were resolved. We have previously described the isolation of a 51/50 kDa protein with starch branching activity from one of these fractions. From three other fractions, we have now partially purified starch branching enzymes corresponding to forms I, IIa and IIb.Keywords
This publication has 16 references indexed in Scilit:
- Differential Expression and Properties of Starch Branching Enzyme Isoforms in Developing Wheat EndospermPlant Physiology, 1997
- Three isoforms of starch synthase and two isoforms of branching enzyme are present in potato tuber starchPlant Science, 1996
- Demonstration of in vitro starch branching enzyme activity for a 51/50‐kDa polypeptide isolated from developing barley (Hordeum vulgare) caryopsesPhysiologia Plantarum, 1996
- Purification of two forms of starch branching enzyme (Q‐enzyme) from developing rice endospermPhysiologia Plantarum, 1992
- Immunological Comparison of the Starch Branching Enzymes from Potato Tubers and Maize KernelsPlant Physiology, 1989
- A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blotsAnalytical Biochemistry, 1984
- Evidence for Independent Genetic Control of the Multiple Forms of Maize Endosperm Branching Enzymes and Starch SynthasesPlant Physiology, 1981
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Multiple forms of (1 → 4)-α-d-glucan, (1 → 4)-α-d-glucan-6- glycosyl transferase from developing zea mays L. KernelsCarbohydrate Research, 1978
- A method for the colorimetric estimation of glycogen with lodineAnalytical Biochemistry, 1962