[Caragana arborescens lectin--a marker of myoepitheliocytes of salivary glands]. / Lektin kory karagany drevovidnoi--marker mioépiteliotsitov sliunnykh zhelez.

Submaxillary salivary gland preparations of a horse, a cow, a pig, a rabbit and white outbred rats were stained with peroxidase-labeled lectins of different carbohydrate specificity. It was found that N-acetyl-D-galactosamine-specific lectins (Caragana arborescens Lam., Phaseolus unatus seeds, Helix pomatia sails) bind selectively with myoepitheliocytes. Best marker of the latter proved to be Caragana arborescens lectin, consisting of two components which differ in their affinity to N-acetyl-D-galactosamine and D-galactose and histochemical properties. Only one of them (the main component, GABA-1) may serve as myoepitheliocyte marker.

[The preparation of an anti-A reagent from the lectin of hairy vetch (Vicia villosa) for detecting antigen A in human erythrocytes and saliva]. / Izgotovlenie reagenta anti-A iz lektina goroshka mokhnatogo dlia vyiavleniia antigena A v éritrotsitakh i sliune cheloveka.

Anti-A reagent for the detection of the relevant antigen in human red cells and saliva has been developed. The reagent is prepared by dissolution of purified Vicia villosa lectin in the serum of group AB or B diluted 8 times with PBS. This solvent appreciably improves the anti-A selectivity of lectin and is used for titration. Purification of lectin by ammonium sulfate precipitation is described. The reagent agglutinates group A red cells in the minimal lectin concentration of 2.5 to 10 micrograms/ml and does not agglutinate group 0 and B red cells in concentration 10 mg/ml. Moreover, the reagent is fit for the detection of antigen A in traces of blood and saliva by the absorption-elution method.

[New fucose-specific lectin from the bark of dwarf almond golden rain Laburnum anagyroides Medik: purification, properties and immunochemical specificity]. / Novyi fukozospetsifichnyi lektin iz kory bobovnika zolotoi dozhd' (Laburnum anagyroides Medik): ochistka, svoistva i immunokhimicheskaia spetsifichnost'.

A new lectin specific towards L-fucose has been purified from the bark of Laburnum anagyroides. The purification procedure included precipitation with ammonium sulfate (30-90% saturation), precipitation of the globuline fraction at pH 4.2, fractionation with rivanol, chromatography on Sephadex G-100 and DEAE-cellulose. Electrophoresis in SDS revealed one protein band with molecular weight of 33,000. The molecular weight of the native lectin is about 130,000, thus suggesting a tetrameric structure of the protein molecule. The lectin obtained contains 13.1% of carbohydrates; its amino acid composition is characterized by a high content of serine, threonine, glutamic and aspartic acids and by a lack of cystine and cysteine. The lectin activity is inhibited by L-fucose (2 mM). Lectin agglutinates native human erythrocytes with a preference for the O(H) blood group. The differences in the titre of hemagglutination of individual erythrocyte samples within a unique blood group were observed.