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      Platelet-activating factor acetylhydrolase (PAF-AH) in human kidney.

      The International journal of biochemistry
      1-Alkyl-2-acetylglycerophosphocholine Esterase, Blood Proteins, metabolism, Calcium, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, physiology, Enzyme Stability, Humans, Hydrogen-Ion Concentration, Kidney Cortex, enzymology, Kidney Medulla, Microsomes, Molecular Weight, Phospholipases A, blood, chemistry, Phospholipases A2, Platelet Activating Factor, analogs & derivatives, Serum Albumin, Bovine, Tissue Distribution, Tissue Preservation

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          Abstract

          1. PAF-AH activity in human kidney (cortex and medulla) has been demonstrated and shares the following properties. 2. Does not require the presence of Ca2+ and appears to be different from phospholipase A2. 3. The pH optimum shows a peak at 7-7.4. 4. It is stable for 4 days at -30 degrees C. 5. It is mainly distributed in the microsomal fraction. 6. The apparent Km values of the enzymes of cortex and medulla are 0.553 and 0.207 microM, respectively and distinct from serum PAF-AH (1.439 microM). 7. The apparent molecular weight values are 60,000 and 25,000 for medulla and cortex, respectively and distinct from serum PAF-AH (94,000).

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