[Carbohydrate-binding proteins--lectins and glycosidases in plants of Anthurium genus]. / Doslidzhennia vuhlevodzv'iazuiuchykh bilkiv--lektyniv ta hlikozydaz u roslyn rodu anturium (Anthurium).

The content of lectins and activity of glycosidases have been estimated in seeds and vegetative organs of 5 strains of plants of Anthurium genus. In seeds of all the investigated strains lectins were detected with the selectivity toward the N-acetyl-galactosamine (minimal inhibitory concentration of sugar was 0.1-0.2 mM) and an anti-A blood group specificity. Lectins of Anthuriums selectively bound O-type glycosidic chains and revealed high affinity toward mucins (salivary or ovary cysts origin). Lectins were not detected in vegetative parts of Anthuriums. In seeds of plants the following glycosidases were detected in the diminishing activity order: alpha-galactosidase, alpha-mannosidase, beta-galactosidase, beta-glucosaminidase.

[Comparative study of the myoglobin of the reindeer Rangifer tarandus, the elk Alces alces and the deer Cervus elaphus xanthopygus]. / Sravnitel'noe izuchenie mioglobinov olenia Rangifer tarandus, losia Alces alces i iziubria Cervus elsphus xenthopygus

Myoglobin preparations from muscles of A. alces, R. tarandus and C. elaphus xanthopygus were isolated by Sephadex gel filtration (G-75). Their Fe content was found to be equal to 0.303--0.308%, which corresponds to the molecular weight of 18, 000. It was shown that splitting of heme from the globin results in an increase of the area occupied by the molecule on the phase boarderline from 36-10(2) to 47-10(2) A2. By the peptide charts method of tryptic hydrolysates combined with the detection of separate amino acid residues in peptides, strong similarities in the primary structure of the myoglobins investigated were found. However, data were obtained which indicate species specificity of this respiratory protein in the animals studied.