| Autor: |
Ceccardi, T.L., Meyer, N.C., Close, T.J. |
| Zdroj: |
Protein Expression and Purification; June 1994, Vol. 5 Issue: 3 p266-269, 4p |
| Abstrakt: |
A maize dehydrin with an apparent molecular weight of 20 kDa was purified from whole kernels of maize inbred line G50. Kernels were ground in a seed mill, stirred overnight in extraction buffer, and centrifuged to extract soluble proteins. The sample was heated to 89°C and centrifuged to remove heat-insoluble proteins. The remaining soluble proteins were fractionated in a three-step chromatographic process. Following cation exchange, hydrophobic interaction, and gel filtration chromatography, pure dehydrin samples were obtained.Copyright 1994, 1999 Academic Press, Inc. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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