The Rhetoric of Fragmentation: Fear and Faith in International Law

International audienceAbstractOver the last decade international lawyers have been increasingly concerned with the `fragmentation' of international law. However, given that this expression has been repeatedly used by the profession since the mid-nineteenth century to depict the state of international law, one may wonder about its recent revival in the international legal discourse. Why has it re-emerged? What can we learn from previous invocations? An answer may be sought by contextualizing the fragmentation debate in a historical perspective. This brings out the repetitive and relatively stylized modes in which the profession has narrated legal developments. This essay suggests a correlation between periods of crisis in general and a critical view of fragmentation on the one hand, and periods of scholarly enthusiasm and the prevalence of positive views about fragmentation on the other. This analysis sheds critical light on both the implicit assumptions and political implications of the current debate on fragmentation

Black cutworm moths after feeding on <i>N. benthamiana</i> plants transformed with the <i>BvSTI</i> gene.

<p>Transformant 11-4, 11-5, 11-6 and 12-2 and untransformed normal control plant. Bar corresponds to 2 cm.</p

Schematic of the reconstructed <i>BvSTI</i> gene in the pCAMBIA1301 transformation vector (pBvSTI).

<p>RB, right border; LB, left border; p35S, cauliflower mosaic virus (CaMV) 35S promoter; <i>hpt</i>, hygromycin phosphotransferase selectable marker gene; NdeI restriction enzyme sites; arrows indicate direction of transcription from the p35S promoter. Horizontal bar indicates the 400-bp fragment of the <i>BvSTI</i> gene used as a probe for Southern blots.</p

Weights of tobacco hornworm larvae feeding on <i>N. benthamiana</i> T2 homozygous plants transformed with the <i>BvSTI</i> gene.

<p>Values represent mean larval weight ± SE (g).</p><p>Means followed by the same superscript within columns are not significantly different (<i>P</i><0.05) by one-way ANOVA test. Number in parenthesis indicates the number of living larvae out of 5 that were weighed.</p

Fall armyworm pupae from feeding bioassays on <i>N. benthamiana</i> plants transformed with the <i>BvSTI</i> gene.

<p>Transformant 11-5, 11-6 and 12-2 and untransformed normal control plant. Bar corresponds to 1 cm.</p

Tobacco hornworm moths after feeding on <i>N. benthamiana</i> plants transformed with the <i>BvSTI</i> gene.

<p>Transformant 11-4, 11-6 and 11-13 and untransformed normal control plant. Bar corresponds to 2 cm.</p

Weights of black cutworm feeding on leaves from <i>N. benthamiana</i> BvSTI T2 homozygous plants.

<p>Values represent mean larval weight ± SE (mg).</p><p>Means followed by the same superscript within columns are not significantly different (<i>P</i><0.05) by one-way ANOVA test. Number in parenthesis indicates the number of living larvae out of 5 that were weighed.</p>†<p>data was not included in the statistical analysis at 7 days since only 1 larvae was weighed, the other 4 pupated.</p

Beet armyworm pupae and emerged moths from feeding bioassays on <i>N. benthamiana</i> plants transformed with the <i>BvSTI</i> gene.

<p>Transformant 11-4, 11-5, 11-6, 11-13 and 12-2 and untransformed normal control plant. Bar corresponds to 1 cm.</p

Immunoblot and in gel analysis of trypsin inhibitor activity in <i>N. benthamiana</i> plants transformed with the <i>BvSTI</i> gene.

<p>A) Immunoblot analysis of <i>BvSTI</i> transformed plants 11-4, 11-6, 11-13 and 12-2 (lane 1–4, respectively) and normal untransformed plant (lane 5) using BvSTI specific antibody. Lane 6, positive control for BvSTI peptides (5 ug of each peptide) used for production of the anti BvSTI-specific antibody; peptides were loaded 60 min after beginning of electrophoresis. Lane, 7, molecular weight standards in kDa. B). In gel analysis of trypsin inhibitor activity. Lane 1–5, <i>BvSTI</i> transformant 11-4, 11-5, 11-6, 11-13 and 12-2, respectively; lane 6, untransformed normal control plant; lane 7, positive control, soybean Kunitz trypsin inhibitor protein, 20 kDa, 0.5 µg.</p