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Chromatographic Resolution of Lysozyme Variants by Jodi Fausnaugh-Pollitt; Gerladine Thevenon; Linda Janis; Fred E. Regnier is a Chemistry article available to read on EtoBox.

What is Chromatographic Resolution of Lysozyme Variants about?

There are seven avian lysozyme variants of nearly identical three-dimensional structure which have amino acid substitutions broadly distributed on their surface. By using these protein variants, it was possible to study the relationship between protein structure and chromatographic retention. It was determined that according to the mode of separation various regions of the proteins surface determine chromatographic retention. At one extreme, immunosorbents targeted a very small region on the protein surface. Hydrophobic interaction chromatography was an intermediate case in which one surface domain of the lysozymes controlled chromatographic behavior. At the opposite extreme, cation-exchange columns probed most of the protein surface. It was concluded that identification of random variations in protein structure will be most successfully detected by a separation mode that broadly targets the surface of a protein.

Who reads Chromatographic Resolution of Lysozyme Variants?

Author

Jodi Fausnaugh-Pollitt; Gerladine Thevenon; Linda Janis; Fred E. Regnier

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1873-3778)

Published

1988

Language

EN

Field

Chemistry (Physical Sciences)