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Crystal structure of a plant albumin from Cicer arietinum (chickpea) possessing hemopexin fold and hemagglutination activity.

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CONCLUSIONS Crystal structure of a reported PA2 albumin from Cicer arietinum shows that it belongs to hemopexin fold family, has four beta-propeller motifs and possesses hemagglutination activity, making it different from known legume lectins. A plant albumin (PA2) from Cicer arietinum, presumably a

Extraction and characterization of chickpea (Cicer arietinum) albumin and globulin.

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Albumin and globulin fractions of 1 Desi and 2 Kabuli varieties of chickpeas (Cicer arietinum) were extracted with water and salt solutions (K(2)SO(4) and NaCl). The extractable yields and particularly the albumin-globulin ratio varied greatly with the extraction medium and chickpea variety.

Nutritional responses of rats to diets based on chickpea ( Cicer arietinum L.) seed meal or its protein fractions.

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The aim of this study was to isolate the protein fractions from chickpea, var. IAC-Marrocos, as well as to evaluate its in vivo nutritional protein quality. Among the proteins, albumins showed better nutritional value in the in vivo assays and amino acid contents, despite their higher trypsin

Identification and Characterization of IgE-reactive Proteins and a New Allergen (Cic a 1.01) from Chickpea (Cicer arietinum)

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Scope: Chickpea (Cicer arietinum) allergy has frequently been reported particularly in Spain and India. Nevertheless, chickpea allergens are poorly characterized. We aimed to identify and characterize potential allergens from

Properties of a lectin purified from the seeds of Cicer arietinum.

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A lectin was isolated from seed extracts of Cicer arietinum by (NH4)2SO4 precipitation and subsequent ion exchange chromatography and gel filtration. Affinity chromatography on desialylated human IgM coupled to AH-Sepharose was also performed, but the amount bound was very low. The lectin has a

Changes in digestibility of proteins from chickpeas (Cicer arietinum L.) germinated in presence of selenium and antioxidant capacity of hydrolysates.

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Germination in the presence of selenium (Se) is an alternative to increase the healthy properties of seeds. This study aimed to compare the Se accumulation in different protein fractions from germinated chickpea (Cicer arietinum L.) and the effect on digestibility and cellular antioxidant activity

Purification, characterization and allergenicity assessment of 26kDa protein, a major allergen from Cicer arietinum.

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Chickpea (CP), a legume of the family Fabaceae, is an important nutrient-rich food providing protein, essential amino acids, vitamins, dietary fibre, and minerals. Unfortunately, several IgE-binding proteins in CP have been detected that are responsible for allergic manifestations in sensitized

Analysis of root proteome unravels differential molecular responses during compatible and incompatible interaction between chickpea (Cicer arietinum L.) and Fusarium oxysporum f. sp. ciceri Race1 (Foc1).

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BACKGROUND Vascular wilt caused by Fusarium oxysporum f. sp. ciceri Race 1 (Foc1) is a serious disease of chickpea (Cicer arietinum L.) accounting for approximately 10-15% annual crop loss. The fungus invades the plant via roots, colonizes the xylem vessels and prevents the upward translocation of

Seed protein fractions and amino acid composition in gram (Cicer arietinum).

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Six chickpea strains were analysed for their protein content and various protein fractions. The protein content ranged from 20.9-25.27%. Albumin, globulin, prolamin and glutelin contents ranged from 8.39-12.31%; 53.44-60.29%; 3.12-6.89% and 19.38-24.40% respectively. Salt soluble proteins (albumin +

Effect of zinc supplementation from different sources on growth, nutrient digestibility, blood metabolic profile, and immune response of male Guinea pigs.

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Forty weaned male guinea pigs of 208.20 +/- 6.62 g mean body weight were divided into 4 groups of 10 animals in a randomized block design. All of the guinea pigs were fed a basal diet [25% ground maize hay, 30% ground maize grain, 22% ground chickpea (Cicer arietinum L.), 9.5% deoiled rice bran, 6%

Sulphur and nitrogen nutrition influence the response of chickpea seeds to an added, transgenic sink for organic sulphur.

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In order to increase the concentration of the nutritionally essential sulphur amino acids in seed protein, a transgene encoding a methionine- and cysteine-rich protein, sunflower seed albumin (SSA), was transferred to chickpeas (Cicer arietinum L). Transgenic seeds that accumulated SSA contained

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