A scientist studying the sequence of the homodimer of lpl would most likely expect that: Lipoprotein lipase.
In order to release fatty acid nutrition for essential tissues, lipoprotein lipase (LPL), which hydrolyzes the triglycerides in lipoproteins, plays a crucial function in plasma lipid metabolism. Adipocytes and myocytes produce LPL, which is then secreted into the interstitial spaces. GPIHBP1, a protein found on endothelial cells, then binds to LPL and transports it to the capillary lumen, where it acts. LPL has been believed to be a homodimer for many years, with dimerization being necessary for both secretion and catalytic activity. The idea that LPL is a homodimer was reviewed in this study. Our results show that monomeric LPL and LPL coupled to GPIHBP1 are both functional.
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