Key result
Human and bovine LPL exhibit structural differences in active domains alongside unrecognized bovine preparation contaminants.
Population
Human and bovine lipoprotein lipase (LPL) preparations from milk and post-heparin plasma
Design
Preclinical
Authors
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Bovine LPL preparations should not substitute for human enzyme in research; leaves open validity of prior studies using bovine sources.
There are significant structural differences between human and bovine lipoprotein lipase enzymes, and commonly used bovine milk LPL preparations may contain unrecognized contaminants.
Goldberg et al. (1986) studied this question. Human lipoprotein lipase vs. Bovine lipoprotein lipase was evaluated on Immunological cross-reactivity and substrate specificity. Human and bovine lipoprotein lipase exhibit significant structural differences in domains involved in enzymatic activity, and bovine milk LPL preparations may contain an unrecognized contaminant.
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