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moluccella laevis/carbohydrate
Link salvestatakse lõikelauale
5 tulemused
Further characterization of some heterophile agglutinins reacting with alkali-labile carbohydrate chains of human erythrocyte glycoproteins.
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Logi sisse
The nature of the receptor sites for several agglutinins is characterized by hemagglutination inhibition assays. The inhibitory activity of human erythrocytes glycoproteins, from which sialic acid, sialic acid and galactose or alkali-labile oligosaccharides have been removed, is compared to the
Immunochemical studies on the combining site of the A + N blood type specific Moluccella laevis lectin.
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Logi sisse
The specificity of the anti A+N lectin of Moluccella laevis (MLL) was examined by hemagglutination experiments with enzyme-modified human erythrocytes and by inhibition of hemagglutination. In addition, binding to various glycoproteins and inhibition by different sugars and glycoproteins were
Isolation, by affinity chromatography and gel filtration in 8 M-urea, of an active subunit from the anti-(blood-group A+N)-specific lectin of Moluccella laevis.
Ainult registreeritud kasutajad saavad artikleid tõlkida
Logi sisse
The lectin from Moluccella laevis seeds agglutinates specifically blood-type-A and -N erythrocytes, and both activities are inhibited by micromolar concentrations of N-acetyl-D-galactosamine. The lectin consists of three subunits: a 67 kDa heterodimer, made up of two S-S-linked polypeptides of 28
Dramatic saccharide-mediated protection of chaotropic-induced deactivation of concanavalin A.
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Logi sisse
This work provides evidence of a physical instance in which some proteins that are usually inactivated under strong chaotropic conditions may become fully resistant through the occupancy of their binding sites with suitable ligands. In this regard, we found that Moluccella laevis lectin remains
Use of O-glycosylation-defective human lymphoid cell lines and flow cytometry to delineate the specificity of Moluccella laevis lectin and monoclonal antibody 5F4 for the Tn antigen (GalNAc alpha 1-O-Ser/Thr).
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Logi sisse
The Tn antigen (GalNAc alpha 1-O-Ser/Thr) is a disease-related O-linked (mucin-type) carbohydrate neoantigen which is expressed in idiopathic Tn syndrome, AIDS, T-cell lymphoma and in many carcinomas. In the present study, we took advantage of a Tn antigen expressing T-lymphocyte clone derived from
Kõige täiuslikum ravimtaimede andmebaas, mida toetab teadus
- Töötab 55 keeles
- Taimsed ravimid, mida toetab teadus
- Maitsetaimede äratundmine pildi järgi
- Interaktiivne GPS-kaart - märgistage ürdid asukohas (varsti)
- Lugege oma otsinguga seotud teaduspublikatsioone
- Otsige ravimtaimi nende mõju järgi
- Korraldage oma huvisid ja hoidke end kursis uudisteuuringute, kliiniliste uuringute ja patentidega
Sisestage sümptom või haigus ja lugege ravimtaimede kohta, mis võivad aidata, tippige ürdi ja vaadake haigusi ja sümptomeid, mille vastu seda kasutatakse.
* Kogu teave põhineb avaldatud teaduslikel uuringutel
