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Article

Purification, analysis, and enzymatic activity of recombinant human synovial fluid phospholipase A2 and N-terminal variants.

Journal of biochemistry - 1 Sept 1992

Di Marco S, Märki F, Hofstetter H, Schmitz A, van Oostrum J, Grütter M G

Abstract excerpt

Recombinant human synovial fluid phospholipase A2 (rPLA2) and several variants with N-terminal sequences modified by addition or deletion of one or two amino acid residues (ala or Met; Des-Asn1, Leu2) have been expressed in mammalian cells and in Escherichia coli, respectively, purified to homogeneity, and characterized. The observed values for the molecular mass of rPLA2 and variants are in complete agreement...

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PMID: 1429522
DOI: 10.1093/oxfordjournals.jbchem.a123904

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