Disease relevance of LjRH101

• Utilizing a simple peroxidase technique applicable to formalin-fixed, paraffin-embedded tissue, lectin binding was studied in 13 cases of Hodgkin's disease [1].
• The binding of peroxidase-labelled lectins to human breast epithelium. III--Altered fucose-binding patterns of breast carcinomas and their significance [2].
• Two peroxidase-labeled lectins, from Tetragonolobus lotus and from peanut (Arachis hypogaea), were used in the study of five cases of polycystic kidney of different types [3].
• Histochemical study of Hurler's disease by the use of peroxidase-labelled lectins [4].
• Abnormal fucosylation of ileal mucus in cystic fibrosis: I. A histochemical study using peroxidase labelled lectins [5].

High impact information on LjRH101

• Lectins conjugated with either peroxidase or ferritin were used to detect specific monosaccharide residues on the luminal front of he fenestrated endothelium in the capillaries of murine pancreas and intestinal mucosa [6].
• Using a simple peroxidase technique applicable to formalin-fixed, paraffin-embedded tissue, the binding properties of five lectins were investigated: concanavalin A (Con A), Arachis hypogaea (peanut agglutinin), Lotus tetragonolobus (asparagus pea), Glycine max (soybean agglutinin) and Bandeiraea simplicifolia [7].
• Lectin receptors as markers of lymphoid cells. I. Demonstration in tissue section by peroxidase technique [7].
• Paraffin-embedded tissue sections were exposed to eight lectin peroxidase conjugates: Dolichos biflorus, Triticum vulgaris, Concanavalin A, Ricinus communis type 2, Arachis hypogaea, Ricinus communis type 1, Tetragonolobus purpureas and Ulex europeus [8].
• The binding of peroxidase-labelled lectins to human breast epithelium. I--Normal, hyperplastic and lactating breast [9].

Biological context of LjRH101

• Peroxidase-labelled lectins were used, since they detect sugar residues of membrane glycoconjugates which play an important role in cell differentiation [10].

Anatomical context of LjRH101

• Histochemical evaluation of secretory glycoproteins in human salivary glands with lectin-horseradish peroxidase conjugates [11].
• Paraffin sections of submandibular, sublingual, minor salivary, and parotid glands from ten human autopsy cases were stained with a battery of ten lectins conjugated to horseradish peroxidase [11].
• Twelve specimens of resin-embedded human trabecular meshwork were probed with a panel of 21 biotinylated lectins, using an avidin-biotin peroxidase revealing system, in order to determine the normal pattern of saccharide expression in this tissue [12].
• Cellular carbohydrate components in human, rabbit and rat lacrimal gland. Studies using fluorescein and peroxidase labelled lectins [13].
• Glycoconjugate distribution on rat gut mucosa has been studied by using peroxidase-labelled lectins (Lotus tetragonolobus, Dolichos biflorus, Arachis hypogaea and Glycine max) after surgical interruption of the common bile duct [14].

Associations of LjRH101 with chemical compounds

• The binding to morphologically normal human retina of eleven biotin- or peroxidase-coupled lectins with different carbohydrate specificities was studied [15].
• Proteins were separated by polyacrylamide gel electrophoresis, transferred to nitrocellulose sheets, reacted with peroxidase-coupled lectins, and detected by color development of the enzyme reaction [16].
• The synthesis during development of fucosyl containing glycoproteins and their presence in an electrophoretic pattern of isolated vitelline coats were also studied using Lotus tetragonolobus (LTA) conjugated with fluorescein and peroxidase [17].
• Slices of aldehyde-fixed lung tissue were labelled with a horseradish peroxidase conjugate of one of the following lectins: Dolichos biflorus lectin, Triticum vulgaris lectin, Canavalia ensiformis lectin (concanavalin A), Limulus polyphemus lectin, Lotus tetragonolobus lectin and Arachis hypogaea lectin [18].
• Secretory products of granular and mucous cells in the gill epithelium of the carp, Cyprinus carpio, were distinguished by their cytochemical reactions with peroxidase-labelled lectins and with the galactose oxidase (GO)-Schiff reagents [19].

Other interactions of LjRH101

• We have identified root hair abundant genes, LjRH101 and LjRH102, from a model legume Lotus japonicus by cDNA-amplified fragment length polymorphism (AFLP) [20].

Analytical, diagnostic and therapeutic context of LjRH101

• Control experiments included perfusion with: (a) unlabeled lectin before lectin conjugate; (b) labeled lectin together with the cognate hapten sugar, and (c) horseradish peroxidase or ferritin alone [6].
• Specimens were fixed by perfusion, and subsequently processed for peroxidase detection and electron microscopy [6].
• Concanavalin A and WGL were separated by isoelectric focusing and detected on blots with horseradish peroxidase and avidin-peroxidase, respectively [21].
• The enzymes alkaline phosphatase, gamma-glutamyltranspeptidase, peroxidase, and beta-glucuronidase were localized in glandular and surface epithelia in frozen sections and in colonies of epithelial cells in culture [22].

References