| The purification of peptides by partition chromatography based on a hydrophobicity scale. | |
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MedLine Citation:
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PMID: 422324 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A study of the efficiency of partition chromatography for the purification of peptides as a function of structure has been undertaken. A series of 19 omission analogs of camel beta-endorphin and of some of its partial sequences have been synthesized with each analog missing only a single amino acid. Their chromatographic properties have been examined with use of the Martin hypothesis and the RM concept, and a hydrophobicity scale for the amino acid side chains was obtained. To a first approximation a correlation with the Tanford hydrophobicity scale for amino acids was found. A decrease in hydrophobicity has been observed with increasing chain length and is discussed in terms of column efficiencies required for the purification of synthetic peptides. |
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Authors:
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D Yamashiro |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: International journal of peptide and protein research Volume: 13 ISSN: 0367-8377 ISO Abbreviation: Int. J. Pept. Protein Res. Publication Date: 1979 Jan |
Date Detail:
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Created Date: 1979-05-26 Completed Date: 1979-05-26 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0330420 Medline TA: Int J Pept Protein Res Country: DENMARK |
Other Details:
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Languages: eng Pagination: 5-11 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Chromatography / methods* Endorphins / chemical synthesis Models, Chemical Peptides / isolation & purification* |
| Chemical | |
Reg. No./Substance:
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0/Endorphins; 0/Peptides |
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