Literature DB >> 7950370

Purification of a maize dehydrin.

T L Ceccardi1, N C Meyer, T J Close.   

Abstract

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 degrees 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.

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Year:  1994        PMID: 7950370     DOI: 10.1006/prep.1994.1040

Source DB:  PubMed          Journal:  Protein Expr Purif        ISSN: 1046-5928            Impact factor:   1.650


  18 in total

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Review 5.  The continuing conundrum of the LEA proteins.

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Journal:  Naturwissenschaften       Date:  2007-05-04

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8.  Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure.

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Journal:  Plant Physiol       Date:  2003-03       Impact factor: 8.340

9.  Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea.

Authors:  A M Ismail; A E Hall; T J Close
Journal:  Plant Physiol       Date:  1999-05       Impact factor: 8.340

10.  Mimicking the plant cell interior under water stress by macromolecular crowding: disordered dehydrin proteins are highly resistant to structural collapse.

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Journal:  Plant Physiol       Date:  2008-10-10       Impact factor: 8.340

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