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A Calcagni

Publications and source records attributed to A Calcagni.

20 records · Page 2Linked to original sources

Hydrolysis of N-phenylacetyl-a-methyl-alpha-amino acids by benzylpenicillinacylase.

Enzymatic hydrolysis of several racemic N-phenylacetyl-alpha-methyl-alpha-amino acids containing an additional aliphatic, aromatic or polar substitutent on the chiral carbon atom, has been studied by using benzylpenicillinacylase from Escherichia coli A.T.C.C.9637. Both the rate of hydrolysis and the stereoselectivity were found to be considerably lower than in the case of natural alpha-amino acids. Steric and electronic factors in the side chains influencing the stereoselectivity are discussed. Key words. Benzylpenicillinacylase; enzymatic hydrolysis; alpha-methyl-alpha-amino acids.

Amidohydrolases↗

Determination of semduramicin sodium in poultry liver by liquid chromatography with vanillin postcolumn derivatization.

A liquid chromatographic (LC) method is described for the quantitative determination of semduramicin sodium in broiler liver when administered under projected use conditions. For this procedure, semduramicin sodium is extracted from liver with methanolic ammonium hydroxide, separated and concentrated by solid-phase extraction steps, and determined by LC with postcolumn derivatization with vanillin. The mean recovery of drug was 95% over the 40-320 ng/g range, the coefficient of variation was +/- 10% or better, and no interference was observed from commercial polyether ionophores. The minimum level of detection for semduramicin sodium in broiler liver is 25 ng/g.

Animals↗