29 research outputs found

    Studies on Desi and Kabuli Chickpea (Cicer arietinum L.) Cultivars.The Levels of Amylase Inhibitots, Levels of Oligosaccharides and In Vitro Starch Digestibility

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    Amylase inhibitor activity (AIA) of chickpea extracts was investigated usmg pancreatic and salivary amylases. The extracts showed higher inhibitor activity towards pancreatic amylase than salivary amylase..Mean values indicated slightly higher inhibitory activity in desi than kabuli cultivars, though clear-cut differences were..not observed among- the cultivars. While in vitro starch digestibility of meal samples indicated no large differences among desi and kabuli types of chickpea, the mean values of digestibility of- isolated starches of kabuli -types wasp higher than those -of desi types: The mean values of stachyose were higher in desi cultivars. When desi and kabuli types were considered together, stachyose- and raffmose contents were not found significantly related to the concentrations of total soluble sugars while stachyose showed a significant correlation with raftinose

    Clostridium perfringens type A enterotoxin forms mepacrine-sensitive pores in pure phospholipid bilayers in the absence of putative receptor proteins

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    AbstractClostridium perfringens enterotoxin (CPE) is an important cause of food poisoning with no significant homology to other enterotoxins and its mechanism of action remains uncertain. Although CPE has recently been shown to complex with tight junction proteins, we have previously demonstrated that CPE increases ionic permeability in single Caco-2 cells using the whole-cell patch-clamp technique, thereby excluding any paracellular permeability. In this paper we demonstrate that CPE forms pores in synthetic phospholipid membranes in the absence of receptor proteins. The properties of the pores are consistent with CPE-induced permeability changes in Caco-2 cells suggesting that CPE has innate pore-forming ability

    Characterization of a spore-specific protein of the Bacillus cereus group

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    Bc1245 is a monocistronic chromosomal gene of Bacillus cereus ATCC 14579 encoding a putative protein of 143 amino acids identified in this study to have a spore-related function in B. cereus. Bc1245 is highly conserved in the genome of members of the B. cereus group, indicating an important function of the gene in this group of bacteria. Quantitative PCR revealed that bc1245 is transcribed late in sporulation (upon formation of phase-bright spores) and at the same time as the mother cell–specific transcription factor sK. The sK regulon includes structural components of the spore (such as coat proteins), and it is therefore plausible that bc1245 might encode a structural outer spore protein. This was confirmed by detection of BC1245 in exosporium extracts from B. cereus by immunoblotting against BC1245 antiserum

    Characterization of a spore-specific protein of the Bacillus cereus group

    No full text
    Bc1245 is a monocistronic chromosomal gene of Bacillus cereus ATCC 14579 encoding a putative protein of 143 amino acids identified in this study to have a spore-related function in B. cereus. Bc1245 is highly conserved in the genome of members of the B. cereus group, indicating an important function of the gene in this group of bacteria. Quantitative PCR revealed that bc1245 is transcribed late in sporulation (upon formation of phase-bright spores) and at the same time as the mother cell–specific transcription factor sK. The sK regulon includes structural components of the spore (such as coat proteins), and it is therefore plausible that bc1245 might encode a structural outer spore protein. This was confirmed by detection of BC1245 in exosporium extracts from B. cereus by immunoblotting against BC1245 antiserum
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