Aliesterase activity in normal and postheparin human blood sera.
An enzyme with characteristics typical of aliesterase has been found in human blood serum using a gas solid chromatographic assay technique. This conflicts with the findings of several authors that aliesterase is absent in the human blood. Another aliesterase is released into the blood stream after intravenous administration of heparin. Partial purification of the aliesterase in normal (preheparin) and postheparin sera was effected by column chromatography using CM- and DEAE-Sephadex. The preheparin aliesterase and postheparin aliesterase have different pH optima of 7.0 and 8.5 respectively. The preheparin aliesterase activity was very sensitive to sodium fluoride and insensitive to a negatively charged detergent, sodium lauryl sulfate, unlike the postheparin esterase which was highly sensitive to sodium lauryl sulfate and comparatively less sensitive to sodium fluoride.
Aliesterase activity in normal and postheparin human blood sera. An enzyme with characteristics typical of aliesterase has been found in human blood serum using a gas solid chromatographic assay technique. This conflicts with the findings of several authors that aliesterase is absent in the human blood. Another aliesterase is released into the blood stream after intravenous administration of heparin. Partial purification of the aliesterase in normal (preheparin) and postheparin sera was effected by column chromatography using CM- and DEAE-Sephadex. The preheparin aliesterase and postheparin aliesterase have different pH optima of 7.0 and 8.5 respectively. The preheparin aliesterase activity was very sensitive to sodium fluoride and insensitive to a negatively charged detergent, sodium lauryl sulfate, unlike the postheparin esterase which was highly sensitive to sodium lauryl sulfate and comparatively less sensitive to sodium fluoride.