THE PURIFICATION OF PEPTIDES BY PARTITION CHROMATOGRAPHY BASED ON A HYDROPHOBICITY SCALE*
作者:
DONALD YAMASHIRO,
期刊:
International Journal of Peptide and Protein Research
(WILEY Available online 1979)
卷期:
Volume 13,
issue 1
页码: 5-11
ISSN:0367-8377
年代: 1979
DOI:10.1111/j.1399-3011.1979.tb01843.x
出版商: Blackwell Publishing Ltd
关键词: chromatography;β‐endorphin;free energy;hydrophobicity;peptide synthesis
数据来源: WILEY
摘要:
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 β‐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 RMconcept, 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 peptid
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