Document Detail


The purification of peptides by partition chromatography based on a hydrophobicity scale.
MedLine Citation:
PMID:  422324     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
D Yamashiro
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
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:
Created Date:  1979-05-26     Completed Date:  1979-05-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0330420     Medline TA:  Int J Pept Protein Res     Country:  DENMARK    
Other Details:
Languages:  eng     Pagination:  5-11     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Chromatography / methods*
Endorphins / chemical synthesis
Models, Chemical
Peptides / isolation & purification*
Chemical
Reg. No./Substance:
0/Endorphins; 0/Peptides

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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