Pigeonpea nutrition and its improvement

Pigeonpea (Cajanus cajan [L.] Millsp.), known by several vernacular and names such as red gram, tuar, Angola pea. yellow dhal and oil dhal, is one of the major grain legume crops of the tropics and sub-tropics. It is a crop of small holder dryland fmmers because it can grow well under subsistence level of agriculture and provides nutritive food, fodder, and fuel wood. It also improves soil by fixing atmospheric nitrogen. India by far is the largest pigeonpea producer it is consumed as decorticated split peas, popularly called as 'dhaL' In other countries, its consumption as whole dty and green vegetable is popular. Its foliage is used as fodder and milling by-products [onn an excellent feed for domestic animals. Pigeonpea seeds contain about 20-22% protein and appreciable amounts of essential amino.acids and minerals. DehuHing and boiling treatments of seeds get rid of the most antinutritional factors as tannins and enzyme inhibitors. Seed storage causes considerable losses in the quality of this legume. The seed protein of pigeonpea has been successfully enhanced by breeding from 20-22% to 28-30%. Such lines also agronomically performed well and have acceptable and color. The high-protein lines were found nutritionally superior to the cultivars because they would provide more quantities of utilizable protein and sulfur-containing amino acids

Differential subcellular localization of endogenous and transfected soluble epoxide hydrolase in mammalian cells: evidence for isozyme variants

Endogenous, constitutive soluble epoxide hydrolase in mice 3T3 cells was localized via immunofluorescence microscopy exclusively in peroxisomes, whereas transiently expressed mouse soluble epoxide hydrolase (from clofibrate-treated liver) accumulated only in the cytosol of 3T3 and HeLa cells. When the C-terminal lie of mouse soluble epoxide hydrolase was mutated to generate a prototypic putative type 1 PTS (-SKI to -SKL), the enzyme targeted to peroxisomes. The possibility that soluble epoxide hydrolase-SKI was sorted slowly to peroxiosmes from the cytosol was examined by stably expressing rat soluble epoxide hydrolase-SKI appended to the green fluorescent protein. Green fluorescent protein soluble epoxide hydrolase-SKI was strictly cytosolic, indicating that -SKI was not a temporally inefficient putative type 1 PTS. Import of soluble epoxide hydrolase-SKI into peroxisomes in plant cells revealed that the context of -SKI on soluble epoxide hydrolase was targeting permissible. These results show that the C-terminal -SKI is a non-functional putative type 1 PTS on soluble epoxide hydrolase and suggest the existence of distinct cytosolic and peroxisomal targeting variants of soluble epoxide hydrolase in mouse and rat