[Synthesis and study of biospecific sorbents for isolating and purifying L-asparaginase from Escherichia coli].
Amino acid and oligoamide derivatives of D-asparagine and L-asparaginic acid (L-asparaginase inhibitors) have been synthesized. An increase in the hydrophobic capacity of the modified inhibitor increases the inhibition constant. Once the modified inhibitor binds with Sepharose 6B, the length of the spacer (a chain of atoms attaching the inhibitor to the polymer matrix) determines affinity of the sorbent for L-asparaginase. On these sorbents affinity shifts from pH optimum of the enzyme activity to pH 4-5. The enzyme of E. coli L-asparaginase has been purified.
D000577:Amides / Q000737:chemistry*; D000596:Amino Acids / Q000737:chemistry*; D001215:Asparaginase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D001216:Asparagine / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D012685:Sepharose; D013379:Substrate Specificity
D000577:Amides; D000596:Amino Acids; D001216:Asparagine; D012685:Sepharose; D001215:Asparaginase
Sintez i izuchenie biospetsificheskikh sorbentov dlia vydeleniia i ochistki L-asparaginazy Escherichia coli.