. 2000 Dec;182(24):6906–6912. doi: 10.1128/jb.182.24.6906-6912.2000

TABLE 3.

Comparison of specific activity of sspF-lacZ product from spores of different B. subtilis strains

Strain	Major SASP^a	Sp act of sspF-lacZ product^b
PS848	α and β	1.8 ± 0.3
PS850	None	5.6 ± 1.2
PS1612	α, β, and SspC^w^t	1.7 ± 0.3
PS1613	SspC^w^t	1.8 ± 0.3
PS1614	α, β, and SspC^a^l^a	2.2 ± 0.4
PS1615	SspC^a^l^a	6.8 ± 1.5

The major SASP noted are only the α/β-type SASP.

Aliquots of 36-h cultures in 2× SG medium were extracted with urea and sodium dodecyl sulfate to remove spore coats and inactivate enzymes not in spores. Spores were then disrupted with lysozyme, and extracts were assayed for β-galactosidase and glucose dehydrogenase. The sspF-lacZ product-specific activities are given as the ratio of the ΔOD₄₂₀/30 min/0.3 ml extract in the β-galactosidase assay to the ΔOD₃₄₀/2 min/0.1 ml extract in the glucose dehydrogenase assay and are averages of duplicate assays on spores from three separate experiments. Values for β-galactosidase in spores without a lacZ fusion have been subtracted from those for β-galactosidase-specific activity; in all cases this value was less than 10% of that in spores with an sspF-lacZ fusion.