TY - JOUR
T1 - Effect of purification protocol on the functional properties of erythrocyte membrane protein 4.1
AU - Workman, Ryan F.
AU - Low, Philip S.
N1 - Funding Information:
1Supported by NIH Research Grant GM24417. 2To whom correspondence should be addressed.
PY - 1998/2
Y1 - 1998/2
N2 - 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.
AB - 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.
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U2 - 10.1006/prep.1997.0812
DO - 10.1006/prep.1997.0812
M3 - Article
C2 - 9473463
AN - SCOPUS:0032004885
SN - 1046-5928
VL - 12
SP - 100
EP - 104
JO - Protein Expression and Purification
JF - Protein Expression and Purification
IS - 1
ER -