Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Determination of PAF-2-acylhydrolase activity

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6898869
A simple and rapid procedure has been developed to determine the PAF-2-acylhydrolase activity in various biological fluids. The assay was based upon the following biophysical properties of PAF (1-O-hexadecyl-2-/sup 3/H-acetyl-sn-glycero-3-phosphocholine, 10 Ci/mMole). In aqueous solution PAF is not soluble below its critical micellar concentration (1.1 ..mu..M) unless albumin (2.5 mg/ml) is present which binds and stabilizes PAF in solution. However, upon precipitation of the albumin with trichloroacetic acid (TCA), 100% of the PAF also co-precipitates. Thus, in a reaction mixture to assess PAF-2-acylhydrolase activity conducted in the presence of albumin, termination of the reaction by the addition of TCA (10% final concentration) precipitates all residual PAF and also inactivates all PAF-2-acylhydrolase activity. Under these conditions 100% of the released /sup 3/H-acetate is recovered in the supernatant after centrifugation, 10,000 x g for 60 sec. Therefore, determination of released /sup 3/H-acetate provides a highly accurate and reproducible measurement of both substrate (PAF) and product (/sup 3/H-acetate) concentrations. Kinetic studies assessing the PAF-2-acylhydrolase in human serum diluted in Hank's balance salt solution containing 2.5 mg/ml human albumin, pH 7.20 yielded an apparent Km = 5 nM.
Research Organization:
Univ. of Texas Health Science Center, San Antonio
OSTI ID:
6898869
Report Number(s):
CONF-8604222-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:4
Country of Publication:
United States
Language:
English