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lens culinaris/albúmina
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Purification, identification and preliminary crystallographic studies of a 2S albumin seed protein from Lens culinaris.
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Lens culinaris (lentil) is a widely consumed high-protein-content leguminous crop. A 2S albumin protein (26.5 kDa) has been identified using NH(2)-terminal sequencing from a 90% ammonium sulfate saturation fraction of total L. culinaris seed protein extract. The NH(2)-terminal sequence shows very
Biochemical and functional characterization of an albumin protein belonging to the hemopexin superfamily from Lens culinaris seeds.
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The present paper reports the purification and biochemical characterization of an albumin identified in mature lentil seeds with high sequence similarity to pea PA2. These proteins are found in many edible seeds and are considered potentially detrimental for human health due to the potential
Fractionation of lentil seeds (Lens culinaris Medik.) for insecticidal and flavonol tetraglycoside components.
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Crude methanol extracts from four cultivated varieties of mature lentil seeds (Lens culinaris Medik.) were found to possess antifeedant and insecticidal properties in laboratory tests with the rice weevil (Sitophilus oryzae L.), an insect pest of stored products. Flash chromatography with silica gel
In vivo binding partners of the Lens culinaris lectin.
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The immobilized lectin from the lentil (Lens culinaris) specifically binds two fractions out of the L. culinaris seed globulins. Both fractions are displaced from the lectin at low pH values. In addition, fraction I fails to interact at high ionic strengths, and fraction II in the presence of
Clinical Significance of Preoperative Hepatocellular Carcinoma With High Lens culinaris Agglutinin-reactive Fraction of Alpha-Fetoprotein, But Low Alpha-Fetoprotein.
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Screening for proteinuria in cats using a conventional dipstick test after removal of cauxin from urine with a Lens culinaris agglutinin lectin tip.
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Proteinuria is an important indicator of urinary tract disease and urine dipsticks are simple and sensitive tools to screen for this marker. However, the use of dipsticks to screen for proteinuria may not be appropriate in cats, since cauxin, a 70 kDa glycoprotein, is secreted by the kidneys in
Clinical evaluation of lens culinaris agglutinin-reactive alpha-fetoprotein and des-gamma-carboxy prothrombin in histologically proven hepatocellular carcinoma in the United States.
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There is no established clinical role for the lens culinaris agglutinin-reactive fraction of alpha-fetoprotein (AFP-L3%) and des-gamma-carboxy prothrombin (DCP) in the management of the U.S. hepatocellular carcinoma (HCC) patient population. In order to clarify the clinical usefulness and
Nutritional utilization by the rat of diets based on lentil (Lens culinaris) seed meal or its fractions.
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The nutritional effects in the rat of raw lentil meal or its fractions have been evaluated in three feeding trials. Growth, gain/feed ratio, apparent N digestibility, and N retention were significantly (p < 0.05) reduced by the inclusion of whole lentil meal, dehulled lentil meal, or
In vitro protein digestibility and physico-chemical properties of flours and protein concentrates from two varieties of lentil (Lens culinaris).
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The chemical composition of whole lentil flours and lentil protein concentrates prepared by alkaline extraction and iso-electric precipitation from Blaze and Laird varieties of lentil were studied. The protein composition of the flours and concentrates, determined by sodium dodecyl sulphate
Impact of heat stress during seed filling on seed quality and seed yield in lentil (Lens culinaris Medikus) genotypes.
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BACKGROUND
Lentil, a cool-season food legume, is highly sensitive to high temperatures, which drastically reduce biomass and seed yield. The effects of heat stress on qualitative and quantitative aspects of seeds are not yet known.
RESULTS
In this study, we assessed the effects of high temperatures
Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin.
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A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-binding Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found
Determination of the carbohydrate-binding site of Bauhinia purpurea lectin by affinity chromatography.
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To determine the carbohydrate-binding site of Bauhinia purpurea lectin (BPA), a D-galactose- and lactose-binding lectin, a peptide which interacts with lactose was purified from endoproteinase Asp-N digests of BPA by chromatography on a lactose-Sepharose column. It consists of nine amino acids and
Lectin-binding characteristics of human natural killer cells.
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Human natural killer (NK) cells separated initially by density centrifugation of lymphocytes (E+) forming rosettes with sheep red blood cells (SRBC), were further fractionated on gradients of bovine serum albumin (BSA). Low density fractions contained effector cells which displayed high cytotoxicity
Binding of mammalian beta 2-microglobulin by glycoproteins in fish serum.
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The results demonstrate the presence in cod serum of beta 2-microglobulin (beta 2m)-binding molecules. Upon fractionation on Sephadex G-200, the bound beta 2m appears mainly in the void volume, but also as a minor peak with the apparent size of albumin. The complexes show affinity to Con A-Sepharose
Distinct molecular species of human alpha-fetoprotein due to differential affinities to lectins.
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Resolution of human alpha-fetoprotein (AFP) into four distinct molecular species was demonstrated by a combination of two affinity chromatographies with crossed-immuno-affino-electrophoresis (CIAE) using concanavalin A (Con A) and Lens culinaris hemagglutinin (LcH)-A and LcH-B as affinity media. Of
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