Publication Date:
1987-10-16
Description:
Chromatographic retention is determined by a relatively small number of amino acids located in a chromatographic contact region on the surface of a polypeptide. This region is determined by the mode of separation and the amino acid distribution within the polypeptide. The contact area may be as small as a few hundred square angstroms in bioaffinity chromatography. In contrast, the contact region in ion exchange, reversed phase, hydrophobic interaction and the other nonbioaffinity separation modes is much broader, ranging from one side to the whole external surface of a polypeptide. Furthermore, structural changes that alter the chromatographic contact region will alter chromatographic properties. Thus, although immunosorbents can be very useful in purifying proteins of similar primary structure, they will be ineffective in discriminating between small, random variations within a structure. Nonbioaffinity columns complement affinity columns in probing a much larger portion of solute surface and being able to discriminate between protein variants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regnier, F E -- GM25431/GM/NIGMS NIH HHS/ -- GM33644/GM/NIGMS NIH HHS/ -- GM34759/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):319-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Purdue University, West Lafayette, IN 47907.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3310233" target="_blank"〉PubMed〈/a〉
Keywords:
Adsorption
;
Amino Acids
;
Chemical Phenomena
;
Chemistry
;
*Chromatography
;
Chromatography, Affinity
;
Chromatography, High Pressure Liquid
;
Chromatography, Ion Exchange
;
Protein Conformation
;
Protein Denaturation
;
*Proteins
;
Recombinant Proteins
;
Surface Properties
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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