PubMed Health⌕ Search

Biomedical subjects

V M Lakhtin

Publications and source records attributed to V M Lakhtin.

24 records · Page 2Linked to original sources
PubMedDate not supplied

[An affinity chromatography sorbent containing concanavalin A groups immobilized by complex formation with cobalt].

A Spheron-base affinity sorbent containing Concanavalin A (Con A) groupings has been synthesized. Con A was immobilized via the formation of a ternary complex with a stationary ligand (tetrafunctional) triethylene tetramine) and cobalt(III) ions. The inertness of cobalt(III) provided strong binding of Con A to the matrix. The sorbent was tested for the ability to absorb proteins (albumin, lysozyme, heparin, and ribonuclease) and used the isolation of glucosaminidase from the proteolytic complex of the fungus Geotrichum candidum. The purified enzyme was characterized biochemically.

Chromatography, Affinity↗
PubMedDate not supplied

[Molecular organization of lectins].

The review includes the data about structural organization of lectins from plants, bacteria, and animals. Localization and homology of domains responsible of carbohydrate binding, cation metals binding, lipid or hydrophobic substances binding, signal peptides, and other type of domains are described. Families and superfamilies of lectins according to their similarity in primary structure are discussed.

Amino Acid Sequence↗
PubMedDate not supplied

[The purification and properties of an extracellular sialo-specific lectin of Bacillus subtilis 316M].

A simple procedure is proposed for purification of lectin from the culture liquid of non-pathogenic Bacillus subtilis 316M, which includes fractionation with ammonium sulfate and rechromatography on Sepharose CL-6B. The procedure enables a 213-fold purification of lectin with a specific activity of 2560 U/mg protein and 51% recovery in activity. According to gel-filtration through Sepharose the lectin has a molecular weight of 190 kDa. It consists of two types of subunits with hemagglutinating activity. The lectin is highly specific to N-glycolylneuraminic and N-acetylneuraminic acids and fructose 1.6-biphosphate.

Amino Acids↗