This article discusses the needs and challenges of developing good, science-based, simple methods for postharvest handling that can be made available in developing countries. Some of the traditional challenges have been successfully met (i.e. identifying causes and sources of losses for key crops, identifying many potential postharvest technologies of practical use for reducing losses), but many challenges remain. These include the characterization of indigenous crops in terms of their unique postharvest physiology (e.g. respiration rate, susceptibility to water loss, chilling sensitivity, ethylene sensitivity), ascertaining the differences between handling recommendations made for well-known varieties and the needs of local varieties of crops, and determining cost effectiveness of scale-appropriate postharvest technologies in each locale and for each crop. Key issues include building capacity at the local level in postharvest science, university teaching and extension, and continued adaptive research efforts to match emerging postharvest technologies to local needs as these continue to change over time. Development of appropriate postharvest technology relies upon many disciplines that are relevant to the overall success of horticulture, i.e. plant biology, engineering, agricultural economics, food processing, nutrition, food safety, and environmental conservation. The expanding pool of new information derived from postharvest research and outreach efforts in these areas can lead in many directions which are likely to have an impact on relieving poverty in developing countries.

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A membrane bound form of nitric oxide synthase of human erythrocytes that could be activated by insulin was purified to homogeneity by detergent solubilization of the purified membrane preparation of these cells. The purified enzyme (M(r) 230 KD) was found to be composed of one heavy chain (M(r) 135 KD) and one light chain (Mr 95 KD) held together by disulphide bond(s). Scatchard plot analysis of insulin binding to the purified enzyme showed the presence of 2 different populations of the binding sites and the activation were directly related to the hormone binding to the protein. Line weaver Burk plot of the purified enzyme showed that the stimulation of the enzymic activity by insulin was related to the decrease of K(m) with simultaneous increase of V(max). Treatment of the purified enzyme with anti insulin receptor antibody inhibited the activation of the enzyme and the binding of the hormone to the protein. Furthermore NO itself, at low concentration (<0.4 microM) activated the enzyme, but at higher concentration (>0.8 microM) had no effect on the activation. Incubation of the purified enzyme with insulin simultaneously stimulated the tyrosine kinase and nitric oxide synthase activities of the preparations, that could be inhibited by genistein (an inhibitor of tyrosine kinase). These results indicated that the insulin activated nitric oxide synthase could be the insulin receptor itself.

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