[HTML][HTML] Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein
TS Kim, CS Sundaresh, SI Feinstein, C Dodia… - Journal of Biological …, 1997 - ASBMB
A Ca 2+-independent phospholipase A 2 (PLA 2) maximally active at pH 4 and specifically
inhibited by the transition-state analogue 1-hexadecyl-3-trifluoroethylglycero-sn-2-
phosphomethanol (MJ33) was isolated from rat lungs. The sequence for three internal
peptides (35 amino acids) was used to identify a 1653-base pair cDNA clone (HA0683) from
a human myeloblast cell line. The deduced protein sequence of 224 amino acids contained
a putative motif (GXSXG) for the catalytic site of a serine hydrolase, but showed no …
inhibited by the transition-state analogue 1-hexadecyl-3-trifluoroethylglycero-sn-2-
phosphomethanol (MJ33) was isolated from rat lungs. The sequence for three internal
peptides (35 amino acids) was used to identify a 1653-base pair cDNA clone (HA0683) from
a human myeloblast cell line. The deduced protein sequence of 224 amino acids contained
a putative motif (GXSXG) for the catalytic site of a serine hydrolase, but showed no …