Journal
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES
Volume 878, Issue 19, Pages 1549-1554Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jchromb.2010.04.009
Keywords
Bifunctional amylase/protease inhibitor; Affinity chromatography; Ion exchange chromatography; Gel filtration; Sodium dodecyl sulphate-polyacrylamide gel electrophoresis
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An ammonium sulphate fraction (20-60%) of bifunctional amylase/protease inhibitor from ragi (Eleusine coracana) was purified by affinity chromatography to give 6.59-fold purity with 81 48% yield The same ammonium sulphate fraction was also subjected to ion exchange chromatography and was purified 4 28-fold with 75.95% yield The ion exchange fraction was subjected to gel filtration and the inhibitor was purified to 6 67-fold with 67 36% yield Further sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed to check the homogeneity of purified amylase/trypsin inhibitor obtained through affinity. ion exchange and gel chromatography The molecular weight of the inhibitor was found to be 14 kDa. This purified inhibitor was used as affinity ligand for the purification of a commercial preparation of pancreatic amylase Crown Copyright (C) 2010 Published by Elsevier B V All rights reserved
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