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. Author manuscript; available in PMC: 2006 Aug 9.
Published in final edited form as: J Biol Chem. 2000 Jun 30;275(26):19620–19627. doi: 10.1074/jbc.M001333200

Table I. Catalytic constants determined in steady-state conditions for BiP and DnaK in the presence of a synthetic peptide or J-MTJ1.

BiP and DnaK ATPase assays were performed as described under Experimental Procedures, in the absence (basal kcat) or presence of various concentrations of Pep2 (0–2 mm) or J-MTJ1 (0–10 μm).

Proteins Basal kcat kcat Pep2 Stimulation kcat J-MTJ1 Stimulation
min−1 min−1 -fold min−1 -fold
pHis10-BiP 0.20 ± 0.10 0.57 ± 0.14 2.85 0.95 ± 0.14 4.75
pHis10-BiP.ent 0.40 ± 0.09 0.47 ± 0.2 1.20 0.82 ± 0.02 2.05
pHis10-BiP-ent-C19 0.32 ± 0.1 0.62 ± 0.11 1.95 0.67 ± 0.016 2.10
pHis6-BiP 0.34 ± 0.04 0.52 ± 0.06 1.55 0.74 ± 0.09 2.20
pHis6-BiP.ent 0.45 ± 0.06 0.51 ± 0.04 1.15 0.74 ± 0.15 1.65
DnaK 0.05 ± 0.007 NDa NDa 0.40 ± 0.03 8.0
a

ND, not determined.