. Author manuscript; available in PMC: 2010 Jul 1.

Published in final edited form as: Protein Expr Purif. 2009 Feb 20;66(1):107–112. doi: 10.1016/j.pep.2009.02.009

Table 1.

Summary of A _1–40 and A _1–42 purification from 1 L E. coli culture^†

	For A _1–40 preparation				For A _1–42 preparation
Purification step	Volume (ml)	IFABP-A _1–40 (mg)	A _1–40 (mg)	Recovery (%)	Volume (ml)	IFABP-A _1–42 (mg)	A _1–42 (mg)	Recovery (%)
Inclusion bodies dissolved in urea (25,000g supernatant)	50	ND^a	ND^a	ND^a	50	ND^a	ND^a	ND^a
Ni-NTA chromatography	40	40	8.2^b	100	40	40	8.6^b	100
Sephacryl S-200 size exclusion chromatography	80	32	6.6^b	80	80	30	6.4^b	75
Factor Xa cleavage	80	ND^a	ND^a	ND^a	80	ND^a	ND^a	ND^a
Overnight aggregation, ppt dissolved in GdnCl	5	22	6.6^b,^c	ND^a	5	21	6.4^b,^c	ND^a
C18 reverse phase chromatography	9	ND^a	4	49	9	ND^a	3	35

^†

10 g cell (wet weight) cell is obtained from 1 L culture.

Not detemined.

The amount of A is calculated from the mass ratio of A and the fusion protein.

The precipitate is expected to contain the full amount of the A initially present.