lens culinaris/кариес

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The structure of the lentil (Lens culinaris) lectin. Amino acid sequence determination and prediction of the secondary structure.

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The subunit structure and complete amino acid sequence of the lectin extracted from Lens culinaris (LcL) seeds was determined. In previous studies, the primary structure of the alpha-chain (Mr = 5,710) was shown to be homologous to the alpha-chain of the lectin from Pisum sativum, the Vicia cracca

Recombinant production and solution structure of lipid transfer protein from lentil Lens culinaris.

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Lipid transfer protein, designated as Lc-LTP2, was isolated from seeds of the lentil Lens culinaris. The protein has molecular mass 9282.7Da, consists of 93 amino acid residues including 8 cysteines forming 4 disulfide bonds. Lc-LTP2 and its stable isotope labeled analogues were overexpressed in

Biphasic changes of the immunological reactivity in the course of experimental lectin-induced arthritis of rabbits.

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A single injection of Lens culinaris lectin (LcL) into the knee joint cavity of non-sensitized rabbits produces an arthritis with an acute and chronic phase, lasting up to one year. The persistence of the lectin in the joint, related to the strong binding affinity of lectins to glycoproteins of

Analysis of the secretions of the subcommissural organs of several vertebrate species by use of fluorescent lectins.

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The glycoprotein secretions of the subcommissural organ were analyzed with the use of nine fluorescent lectins, specific to different sugar moieties. After exposure to Concanavalin A a bright fluorescence was observed in the ependymal cells of the subcommissural organs of all vertebrates studied

New insights into ligand binding by plant lipid transfer proteins: A case study of the lentil Lc-LTP2

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Lipid transfer proteins (LTPs) are an important class of plant proteins containing an internal cavity and binding hydrophobic ligands. Although LTP structures and functions are well studied, mechanisms of ligand binding remain unclear. Earlier, we discovered the lentil lipid transfer protein Lc-LTP2

Ligand Binding Properties of the Lentil Lipid Transfer Protein: Molecular Insight into the Possible Mechanism of Lipid Uptake.

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The lentil lipid transfer protein, designated as Lc-LTP2, was isolated from Lens culinaris seeds. The protein belongs to the LTP1 subfamily and consists of 93 amino acid residues. Its spatial structure includes four α-helices (H1-H4) and a long C-terminal tail. Here, we report the ligand binding

Ontogenesis of the secretory epithelium of the bovine subcommissural organ. A histofluorescence study using lectins and monoclonal antibodies.

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A spatio-temporal analysis of the differentiation of a group of specialized (secretory) ependymal cells in the subcommissural organ (SCO) of the brain was undertaken in the bovine using a monoclonal antibody (C1B8A8) which is specific of the secretory process in this organ. In addition, lectins

Complex-type glycoproteins synthesized in the subcommissural organ of mammals. Light- and electron-microscopic investigations by use of lectins.

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The secretory activity in the subcommissural organ (SCO) of the sheep and cow was examined by means of lectin histochemistry and cytochemistry. Among the various lectins tested. Concanavalin A (Con A) revealed glycoproteins rich in mannosyl residues in the rough endoplasmic reticulum of ependymal

Induction of polymorphonuclear leukocyte-mediated cytolysis by wheat germ agglutinin and antitumor antibody.

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The role of polymorphonuclear leukocytes (PMNs) as effector cells in tumor lysis was investigated in vitro. PMNs were obtained from the peritoneal cavity of C3H/He Mice injected ip with 2 ml of 12% casein sodium. These PMNs could lyse murine MM46 tumor cells in the presence of the plant lectin,

Nanohoneycomb SERS-active Chip for the Determination of Biomarkers of Hepatocellular Carcinoma.

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Overexpression of the Lens culinaris agglutinin (LCA)-reactive fraction of alpha-fetoprotein is an essential biomarker for early diagnosis of hepatocellular carcinoma (HCC). In this study, we designed a new surface-enhanced Raman spectroscopy (SERS) active chip for the detection of AFP with high

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