cratylia argentea/carbohydrate

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Isolation of a trypsin inhibitor from Echinodorus paniculatus seeds by affinity chromatography on immobilized Cratylia mollis isolectins.

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A highly purified trypsin inhibitor was obtained from Echinodorus paniculatus when an extract prepared from E. paniculatus seed flour (25 gl(-1), with 0.1 M ammonium acetate buffer, pH 8.3, under agitation for 6 min at 28 degrees C) was chromatographed on Sephadex G-25 (12 mlh(-1)), followed by

Crataeva tapia bark lectin is an affinity adsorbent and insecticidal agent.

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Hemagglutinating activity has been associated to presence of lectin, carbohydrate-binding proteins. In this work Crataeva tapia bark lectin (CrataBL) was purified in milligram quantities (28 mg per g of bark) by ion exchange chromatography. The lectin was thermo-stable, ion-independent and

Amino acid sequence and tertiary structure of Cratylia mollis seed lectin.

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Carbohydrate-protein interactions play a key role in many biological processes. Cramoll is a lectin purified from Cratylia mollis seeds that is taxonomically related to concanavalin A (Con A). Although Cramoll and Con A have the same monosaccharide specificity, they have different glycoprotein

Mitogenic activity of Cratylia mollis lectin on human lymphocytes.

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The mitogenic effect of Cratylia mollis seed lectin preparations containing two (Cramoll 1,4) or one molecular form (Cramoll 1) showed activity similar to the well known T-cell mitogen, concanavalin A (Con A). The effect on human lymphocytes was analyzed through a colorimetric assay using

Affinity matrices of Cratylia mollis seed lectins for isolation of glycoproteins from complex protein mixtures.

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This work reports the use of matrices containing Cratylia mollis lectins (Cramoll 1,2,3-Sepharose and Cramoll 3-Sepharose) for isolation of glycoproteins from fetal bovine serum, human colostrum, hen egg white, and human blood plasma. Cramoll 1,2,3-Sepharose was able to bind a glycoprotein from

Histochemical evaluation of human prostatic tissues with Cratylia mollis seed lectin.

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Lectins, proteins which selectively recognize carbohydrates, have been used in histochemistry for the evaluation of changes in glycosylation in processes of cellular differentiation and/or dedifferentiation. Cratylia mollis seed lectins (Cramoll 1,4 and Cramoll 3), conjugated to horseradish

Binding evaluation of Isoform 1 from Cratylia mollis lectin to human mammary tissues.

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The phenomenon of altered carbohydrates in transformed cell surfaces has been studied through histochemical techniques using lectins. Specific binding patterns to normal and transformed mammary tissues were evaluated by Isoform 1 from Cratylia mollis lectin (Cra Iso 1). Protocols using a direct

Ultrastructural analysis and immunocytochemical localization of isolectins in Cratylia mollis seeds.

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Cratylia mollis is a native forage from the semi-arid region of Northeast, State of Pernambuco, Brazil, whose seeds have been considered an important lectin source. Multiple molecular forms of lectins, carbohydrate-binding proteins, have been purified from C. mollis seeds (Cra Iso) allowing several

A lectin from Dioclea violacea Interacts with midgut surface of Lutzomyia migonei, unlike its homologues, Cratylia floribunda lectin and Canavalia gladiata lectin.

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Leishmaniasis is a vector-borne disease transmitted by phlebotomine sand fly. Susceptibility and refractoriness to Leishmania depend on the outcome of multiple interactions that take place within the sand fly gut. Promastigote attachment to sand fly midgut epithelium is essential to avoid being

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