Proteomic Analysis of the Royal Jelly and Characterizationof the Functions of its Derivation Glands in the HoneybeeJ. Proteome Res, Article ASAPTo identify candidate royal jelly (RJ) proteins that mightaffect the physiologic status of honeybee colony members, we used shotgunproteomics to comprehensively identify the RJ proteome as well as proteomes ofthe hypopharyngeal gland (HpG), postcerebral gland (PcG), and thoracic gland(TG), from which RJ proteins are assumed to be derived. We identified a total of 38 nonredundant RJ proteins,including 22 putative secretory proteins and Insulin-like growth factor-bindingprotein complex acid labile subunit. Among them, 9 proteins were newlyidentified from RJ. Comparison of the RJ proteome with the HpG, PcG, and TGproteomes revealed that 17 of the 22 putative secretory RJ proteins werederived from some of these glands, suggesting that the RJ proteome is acocktail of proteins from these three glands. Furthermore, pathway analysissuggested that the HpG proteome represents the molecular basis of the extremelyhigh protein-synthesizing ability, whereas the PcG proteome suggests that thePcG functions as a reservoir for the volatile compounds and a primer pheromone.Finally, to further characterize the possible total RJproteome, we identified putative secretory proteins in the proteomes of thesethree glands. This will be useful for predicting novel RJ protein components infuture studies.
11 Aralık 2012 Salı
38 Royal Jelly Proteins Identified
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Proteomic Analysis of the Royal Jelly and Characterizationof the Functions of its Derivation Glands in the HoneybeeJ. Proteome Res, Article ASAPTo identify candidate royal jelly (RJ) proteins that mightaffect the physiologic status of honeybee colony members, we used shotgunproteomics to comprehensively identify the RJ proteome as well as proteomes ofthe hypopharyngeal gland (HpG), postcerebral gland (PcG), and thoracic gland(TG), from which RJ proteins are assumed to be derived. We identified a total of 38 nonredundant RJ proteins,including 22 putative secretory proteins and Insulin-like growth factor-bindingprotein complex acid labile subunit. Among them, 9 proteins were newlyidentified from RJ. Comparison of the RJ proteome with the HpG, PcG, and TGproteomes revealed that 17 of the 22 putative secretory RJ proteins werederived from some of these glands, suggesting that the RJ proteome is acocktail of proteins from these three glands. Furthermore, pathway analysissuggested that the HpG proteome represents the molecular basis of the extremelyhigh protein-synthesizing ability, whereas the PcG proteome suggests that thePcG functions as a reservoir for the volatile compounds and a primer pheromone.Finally, to further characterize the possible total RJproteome, we identified putative secretory proteins in the proteomes of thesethree glands. This will be useful for predicting novel RJ protein components infuture studies.
Proteomic Analysis of the Royal Jelly and Characterizationof the Functions of its Derivation Glands in the HoneybeeJ. Proteome Res, Article ASAPTo identify candidate royal jelly (RJ) proteins that mightaffect the physiologic status of honeybee colony members, we used shotgunproteomics to comprehensively identify the RJ proteome as well as proteomes ofthe hypopharyngeal gland (HpG), postcerebral gland (PcG), and thoracic gland(TG), from which RJ proteins are assumed to be derived. We identified a total of 38 nonredundant RJ proteins,including 22 putative secretory proteins and Insulin-like growth factor-bindingprotein complex acid labile subunit. Among them, 9 proteins were newlyidentified from RJ. Comparison of the RJ proteome with the HpG, PcG, and TGproteomes revealed that 17 of the 22 putative secretory RJ proteins werederived from some of these glands, suggesting that the RJ proteome is acocktail of proteins from these three glands. Furthermore, pathway analysissuggested that the HpG proteome represents the molecular basis of the extremelyhigh protein-synthesizing ability, whereas the PcG proteome suggests that thePcG functions as a reservoir for the volatile compounds and a primer pheromone.Finally, to further characterize the possible total RJproteome, we identified putative secretory proteins in the proteomes of thesethree glands. This will be useful for predicting novel RJ protein components infuture studies.
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