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. 2012 Nov 30;7(11):e50829. doi: 10.1371/journal.pone.0050829

Table 2. Characterization of the purified NHases, α(StrepP14K)2, R-NHases and R-α(StrepP14K)2.

Protein (plasmid) NHase activity, units/mg Co content (mol of ions/mol of protein) N-terminal sequence of α-subunit
Holo-NHase (pET-A-B-P14K) 439±3.6 0.88±0.06/αβ GQSHTHD
Apo-NHase (pET-A-B-P14K) 18.3±3.2 0.03±0.01/αβ ND*
Holo-NHase (pET-A-B-StrepP14K) 421±6.0 0.89±0.05/αβ ND
Holo-α(StrepP14K)2 (pET-A-B-StrepP14K) 0 0.91±0.01/α(StrepP14K)2 GQSHTHD
Apo-α(StrepP14K)2 (pET-A-B-StrepP14K) 0 0.04±0.01/α(StrepP14K)2 ND
R-apo-NHase 418±5.8 0.87±0.05/αβ ND
R-α(StrepP14K)2 (pET-A-B-StrepP14K) 0 0.90±0.04/α(StrepP14K)2 ND
Holo-NHase(HisT7-α) (pET-HisT7A-B-P14K) 396±8.7 0.89±0.05/αβ ND
Apo-NHase(HisT7-α) (pET-HisT7A-B-P14K) 20.5±4.9 0.04±0.02/αβ GSSHHHH
R-NHase(HisT7-α) 417±8.0 0.87±0.03/αβ GQSHTHD
Holo-NHase (pET-B-A-P14K) 410±6.3 0.89±0.05/αβ ND
*

ND, not detected.

The corresponding expression plasmids are shown in parentheses.