engleski

Partial purification and characterization of N-Acetylmuramyl-L-alanine amidase from human and mouse serum

The enzyme N-acetylmuramyl-L-alanine amidase has been detcted in human, mouse, rabbit, bovine and sheep sera. A method for detection of amidase activity using 14-C-peptidoglycan monomer as the substrate has been developed. Partial purification of human and mouse amidase was achieved by gel chromatography. Both amidase preparations exhibited maximal activity at pH 9.0 in Tris-HCl buffer and required Mg2+ for maximal activity. Following digestion of peptidoglycan monomer, the disaccharide GlcNAc-MurNAc and the corresponding pentapeptide L-Ala-D-isoGln-meso-DAP-D-Ala-D-Ala were formed and subsequently isolated and chemically characterized.

Peptidoglycan monomer; N-Acetylmuramyl-L-alanine amidase; mammalian sera

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