Effect of purification protocol on the functional properties of erythrocyte membrane protein 4.1

Ryan F. Workman, Philip S. Low

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

The inositol hexaphosphate (IHP) method for purification of the erythrocyte membrane protein 4.1 yields the largest quantity of pure protein of any published protocol. However, protein 4.1 isolated by this method was found to bind to KI-stripped inside-out red blood cell membrane vesicles (KIOVs) only 40% as well as protein 4.1 purified by other methods. While an improved Tyler method, the SP method, yields 30-40% less protein 4.1 than the IHP method, the SP preparation nevertheless exceeds the IHP method in that the protein 4.1 is fully functional. Unlike the Tyler method, the SP procedure is also free of contaminating spectrin, p55, and proteases.

Original languageEnglish (US)
Pages (from-to)100-104
Number of pages5
JournalProtein Expression and Purification
Volume12
Issue number1
DOIs
StatePublished - Feb 1998

ASJC Scopus subject areas

  • Biotechnology

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