Purification, analysis, and enzymatic activity of recombinant human synovial fluid phospholipase A sub(2) and N-terminal variants

Recombinant human synovial fluid phospholipase A sub(2) (rPLA sub(2)) and several variants with N-terminal sequences modified by addition or deletion of one or two amino acid residues (Ala or Met; Des-Asn super(1), Leu sub(2)) have been expressed in mammalian cells and in Escherichia coli), respecti...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1992-01, Vol.112 (3), p.350-354
Main Authors: Di Marco, S, Maerki, F, Hofstetter, H, Schmitz, A, van Oostrum, J, Gruetter, M G
Format: Article
Language:English
Subjects:
biochemical characteristics
isoenzymes
man
phospholipase A2
recombinant
synovial fluid
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Summary:Recombinant human synovial fluid phospholipase A sub(2) (rPLA sub(2)) and several variants with N-terminal sequences modified by addition or deletion of one or two amino acid residues (Ala or Met; Des-Asn super(1), Leu sub(2)) have been expressed in mammalian cells and in Escherichia coli), respectively, purified to homogeneity, and characterized. The observed values for the molecular mass of rPLA sub(2) and variants are in complete agreement with the predicted values for a correctly folded structure containing seven disulfide bridges.
ISSN:0021-924X