Structure and properties of a human non-pancreatic phospholipase A2
RM Kramer, C Hession, B Johansen, G Hayes… - Journal of Biological …, 1989 - ASBMB
We have purified a human non-pancreatic phospholipase A 2 that is present in platelets and
is enriched in rheumatoid synovial fluid. The enzyme is calcium-dependent, has a pH
optimum of 8–10, and shows a striking preference for substrate presented in the form of
Escherichia coli membranes. In the E. coli phospholipase A 2 assay the phospholipase
exhibits an apparent specific activity of 300 µmol/mg/min. Using oligonucleotide probes
based on amino-terminal sequence data, we cloned the corresponding human gene from a …
is enriched in rheumatoid synovial fluid. The enzyme is calcium-dependent, has a pH
optimum of 8–10, and shows a striking preference for substrate presented in the form of
Escherichia coli membranes. In the E. coli phospholipase A 2 assay the phospholipase
exhibits an apparent specific activity of 300 µmol/mg/min. Using oligonucleotide probes
based on amino-terminal sequence data, we cloned the corresponding human gene from a …