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. 2002 Apr;68(4):1509–1515. doi: 10.1128/AEM.68.4.1509-1515.2002

TABLE 3.

Binding characteristics of 125I-labeled Cry1 toxins as determined by homologous competition assays using BBMV from whole neonate and third-instar larvaea

Toxin Larvae M. sexta
P. brassicae
M. brassicae
S. exigua
Kcom (nM) Bmax (pmol/mg) Kcom (nM) Bmax (pmol/mg) Kcom (nM) Bmax (pmol/mg) Kcom (nM) Bmax (pmol/mg)
Cry1J Neonateb 80.3 ± 24.6 159 ± 47.3 58 ± 25 94 ± 33 231 ± 109 680 ± 326
Third instarc 61.3 ± 17.16 109 ± 28 39 ± 10 58 ± 14 NDd ND 438 ± 96 1,130 ± 287
Cry1Ca Neonate 7.2 ± 2.6 114 ± 32 2.2 ± 1.9 53 ± 33
Third instar 7.6 ± 2.3 72 ± 18 ND ND 3.4 ± 2.3 172 ± 62 ND ND
Cry1Ac Neonate 103 ± 45 2,988 ± 1,055 415 ± 113 2,556 ± 860
Third instar 25 ± 23 211 ± 189 406 ± 361 1,558 ± 1760 ND ND ND ND
Cry1Ba Neonate 202 ± 85 1,873 ± 812 2.8 ± 2.3, 8.1 ± 5.8, ND ND ND ND
424 ± 189e 1,320 ± 608e
Third instar 105 ± 31.5 738 ± 214 174 ± 46.3 726 ± 207
a

Kcom and Bmax were calculated from a LIGAND analysis of the binding experiment results. The values are means ± standard errors of the means.

b

BBMV were prepared from whole neonate larvae.

c

BBMV were prepared from whole third-instar larvae.

d

ND, not determined.

e

The first value is the value for a high-affinity binding site, and the second value is the value for a low-affinity binding site.