Original citation:Wilson, Kalpana (2015) Towards a radical re-appropriation: gender, development and neoliberal feminism. Development and Change, 46 (4

The mobilization of seed storage proteins upon seed imbibition and germination is a crucial process in the establishment of the seedling. Storage proteins fold compactly, presenting only a few vulnerable regions for initial proteolytic digestion. Evolutionarily related storage proteins have similar three-dimensional structure, and thus tend to be initially cleaved at similar sites. The initial cleavage makes possible subsequent rapid and extensive breakdown catalyzed by endo- and exopeptidases. The proteolytic enzymes that degrade the storage proteins during mobilization identified so far are mostly cysteine proteases, but also include serine, aspartic and metalloproteases. Plants often ensure early initiation of storage protein mobilization by depositing active proteases during seed maturation, in the very compartments where storage proteins are sequestered. Various means are used in such cases to prevent proteolytic attack until after imbibition of the seed with water. This constraint, however, is not always enforced as the dry seeds of some plant species contain proteolytic intermediates as a result of limited proteolysis of some storage proteins. Besides addressing fundamental questions in plant protein metabolism, studies of the mobilization of storage proteins will point out proteolytic events to avoid in large-scale production of cloned products in seeds. Conversely, proteolytic enzymes may be applied toward reduction of food allergens, many of which are seed storage proteins.

This article examines the increasing use of 'positive', active images of 'poor women in developing countries' by development institutions, in relation to several interlinked factors: critiques of earlier representations of 'Third World women' as an essentialised category of 'passive victims'; the appropriation-and transformation-within neoliberal discourses of development from the 1990s onwards of concepts of agency and empowerment; and changes in the role of development NGOs in the same period. Through a discussion of recent publicity campaigns by Oxfam Unwrapped, the Nike Foundation and Divine chocolate, the article examines the specific and gendered ways in which these more recent visual productions are racialised, exploring, in particular, parallels and continuities between colonial representations of women workers and today's images of micro-entrepreneurship within the framework of neoliberal globalisation. The article concludes that, like their colonial predecessors, contemporary representations obscure relations of oppression and exploitation, and work to render collective challenges to the neoliberal model invisible.The ideas in this article have emerged from two interrelated areas of my research: first, an ongoing exploration of questions of 'race' and racism in contemporary development and, second, an analysis of the appropriation and transformation of feminist concepts by neoliberal development discourses. The paper addresses the shift to 'positive images' of women in the global South by international NGOs, donor governments, the World Bank and other development institutions over the past two decades. I provide a preliminary (and necessarily brief) account of how 'race' and racism have historically and conceptually been inscribed in notions of development, and how these processes have been gendered. I go on to describe how, partly in response to Third World feminist critiques, the notion of women's 'agency' has become ubiquitous within approaches to gender and development (GAD), and has been incorporated in neoliberal development discourses, with

Three cysteine proteinase inhibitor cDNA clones (pL1, pR1, and pN2) have been isolated from a soybean (Glycine max 1. Merr.) embryo library. The proteins encoded by the clones are between 60 and 70% identical and contain the consensus QxVxC motif and W residue i n the appropriate spatial context for interaction with the cysteine proteinase papain. L7, R7, and N2 mRNAs were differentially expressed in different organs of plants (juvenile and mature) and seedlings, although NZ mRNA was constitutive only i n flowers. R I and N2 transcripts were induced by wounding or methyl jasmonate (M-JA) treatment in local and systemic leaves coincident with increased papain inhibitory activity, indicating a role for R I and N2 in plant defense. The L I transcript was constitutively expressed in leaves and was induced slightly by M-JA treatment in roots. Unlike the chymotrypsin/trypsin proteinase inhibitor II gene (H. Peiia-Cortes, J. Fisahn, 1. Willmitzer [19951 Proc Natl Acad Sci USA 92: 41 06-41 13), expression of the soybean genes was only marginally induced by abscisic acid and only in certain tissues. Norbornadiene, a competitive inhibitor of ethylene binding, abolished the wounding or M-JA induction of R I and N2mRNAs but not the accumulation of the wound-inducible vspA transcript. Presumably, ethylene binding to its receptor is involved in the wound inducibility of R I and N2 but not vspA mRNAs. Bacterial recombinant L I and R1 proteins, expressed as glutathione S-transferase fusion proteins, exhibited substantial inhibitory activities against vicilin peptidohydrolase, the major thiol endopeptidase i n mung bean seedlings. Recombinant R I protein had much greater cysteine proteinase inhibitor activity than recombinant L I protein, consistent with the wound inducibility of the R7 gene and its presumed role in plant defense.Injury to plants due to phytophagous insects or mechanical damage induces accumulation of proteinase inhibitor proteins (Ryan, 1981(Ryan, , 1990. Inhibitor proteins with specificity against Ser proteinases have been well characterized and there is direct evidence of their involvement in host plant defense against herbivorous insects (Johnson et al.,

The degradation of the major seed storage globulins of the soybean (Glycine max [L.] Merrill) was examined during the first 12 days of germination and seedling growth. The appearance of glycinin and flconglycinin degradation products was detected by sodium dodecyl sulfatepolyacrylamide gel electrophoresis of cotyledon extracts followed by electroblotting to nitrocellulose and immunostaining using glycinin and B-conglycinin specific antibodies. The three subunits of fl-conglycinin were preferentially metabolized. Of the three subunits of j-conglycinin, the larger a and a' subunits are rapidly degraded, generating new #-conglycinin cross-reactive polypeptides of 51,200 molecular weight soon after imbibition of the seed. After 6 days of growth the a-subunit is also hydrolyzed. At least six polypeptides, ranging from 33,100 to 24,000 molecular weight, appear as apparent degradation products of f-conglycinin. The metabolism of the glycinin acidic chains begins early in growth. The glycinin acidic chains present at day 3 have already been altered from the native form in the ungerminated seed, as evidenced by their higher mobility in an alkaline-urea polyacrylamide gel electrophoresis system. However, no change in the molecular weight of these chains is detectable by sodium dodecyl sulfate-polyarylamide gel electrophoresis. Examination of the glycinin polypeptide amino-termini by dansylation suggests that this initial modification of the acidic chains involves limited proteolysis at the carboxyl-termini, deamidation, or both. After 3 days of growth the acidic chains are rapidly hydrolyzed to a smaller (21,900 molecular weight) form. The basic polypeptides of glycinin appear to be unaltered during the first 8 days of growth, but are rapidly degraded thereafter to unidentified products. All of the original glycinin basic chains have been destroyed by day 10 of growth.During the development ofthe dicot seed on the mother plant, storage molecules, particularly starches, proteins, and triglycerides, are laid down in the seed. These reserves are mobilized during germination and seedling growth to supply the energy and metabolic intermediates needed by the seedling prior to the establishment of photosynthetic autotrophism. In the legume seed a relatively large fraction of these reserves, on a weight basis, is composed of storage proteins.The major legume storage proteins are the globulins legumin and vicilin. In the soybean (Glycine max [L.] Merrill) these proteins are called glycinin and fl-conglycinin, respectively.Much work has been done on the structure, biosynthesis, and genetics of these soybean proteins (15,18,20), as well as on their degradation by mammalian trypsin (10-12). However, essen-'Supported by National Science Foundation grant PCM 8301202. A preliminary account of this investigation has been published as Ref. 29. 71 tially no work has been done on their degradation in vivo during germination and seedling growth. We have previously demonstrated that the Bowman-Birk and Kunitz trypsin inhibitor...