Purification of annexin I and annexin II from human placental membranes by high-performance liquid chromatography
KG Moore, F Goulet, AC Sartorelli - Protein Expression and Purification, 1992 - Elsevier
Annexin I and annexin II were extracted from human placental membranes with ethylene
glycol bis (β-amino-oethyl ether)-N, N′-tetraacetic acid (EGTA) and purified by high-
performance liquid chromatography by measuring their ability to inhibit phospholipase A 2
activity in vitro. Neither protein was capable of binding to a DEAE-5PW HPLC column at
neutral pH; however, they were resolved through binding to a Mono S column and passage
through size-exclusion HPLC columns. Annexin I and its covalently linked dimer (36 and 66 …
glycol bis (β-amino-oethyl ether)-N, N′-tetraacetic acid (EGTA) and purified by high-
performance liquid chromatography by measuring their ability to inhibit phospholipase A 2
activity in vitro. Neither protein was capable of binding to a DEAE-5PW HPLC column at
neutral pH; however, they were resolved through binding to a Mono S column and passage
through size-exclusion HPLC columns. Annexin I and its covalently linked dimer (36 and 66 …