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

doi:10.1093/oxfordjournals.jbchem.a123904

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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 homoge...

Topics

Amino Acid Sequence
Animals
CHO Cells
Cloning, Molecular
Cricetinae
Escherichia coli
Genetic Variation
Humans
Molecular Sequence Data
Mutagenesis, Site-Directed
Phospholipases A
Phospholipases A2
Recombinant Proteins
Synovial Fluid

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Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1429522-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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