[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.
D002846:Chromatography, Affinity / Q000295:instrumentation*; D003035:Cobalt / Q000737:chemistry*; D003208:Concanavalin A / Q000737:chemistry*; D005848:Geotrichum / Q000201:enzymology; D006596:Hexosaminidases / Q000302:isolation & purification; D006868:Hydrolysis; D011073:Polyamines / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry
D011073:Polyamines; D011506:Proteins; D003208:Concanavalin A; D003035:Cobalt; D006596:Hexosaminidases
Affinnyĭ khromatograficheskiĭ sorbent, soderzhashchiĭ gruppirovki konkanavalina A, immobilizovannye kompleksoobrazovaniem s kobal'tom.