Recombinant Expression, Purification and Characterisation of the Hmg Domain of Human Sry
| Autor: | Julia Yotis, Vincent R. Harley, Sabine Kelly, Mary Macris |
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| Rok vydání: | 2003 |
| Předmět: |
Male
Calmodulin Protein domain Electrophoretic Mobility Shift Assay Biochemistry law.invention Structure-Activity Relationship chemistry.chemical_compound Structural Biology Transcription (biology) law Escherichia coli Humans chemistry.chemical_classification Binding Sites Chromosomes Human Y biology High Mobility Group Proteins Nuclear Proteins Fast protein liquid chromatography DNA General Medicine Sex Determination Processes Recombinant Proteins Sex-Determining Region Y Protein Protein Structure Tertiary Chromatin Amino acid DNA-Binding Proteins chemistry biology.protein Recombinant DNA Transcription Factors |
| Zdroj: | Protein & Peptide Letters. 10:281-286 |
| ISSN: | 0929-8665 |
| DOI: | 10.2174/0929866033479004 |
| Popis: | The HMG domain is a DNA binding and bending 'architectural' motif involved in chromatin re-modelling during transcription. Recombinant SRY HMG domain protein, 88 amino acids in length, has been produced in E. coli. Using FPLC and a stirred ultra-filtration cell, this domain has been purified to homogeneity and concentrated to yield milligram quantities. Functional characterisation studies of the pure, concentrated SRY HMG domain show the recombinantly expressed protein to be active in terms of DNA binding and calmodulin binding activities. |
| Databáze: | OpenAIRE |
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