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• W2070291088 abstract "Abstract 1. 1. A critical analysis of the difficulties associated with studying the kinetics of palmityl-CoA: monopalmityl- sn -glycerol 3-phosphate palmityltransferase (lysophosphatidic acid acyltransferase or LPAT [EC 2.3.1.-]) from rabbit mammary microsomes is presented. 2. 2. Problems such as non-specific substrate binding to microsomes, bovine serum albumin, and glass; monomer-micelle transition in the substrate concentration range assayed; the presence of a thioesterase [EC 3.1.2.2] enzyme in the microsomes which competes with LPAT for available palmityl-CoA; endogenous donor(s); time lag in the progress curve; product inhibition: and reduced substrate conversion are discussed. 3. 3. These are not unique to the LPAT assay system and the observations are applicable to other systems wherein the enzyme is membrane-bound and active with amphiphilic substrates." @default.
• W2070291088 created "2016-06-24" @default.
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• W2070291088 date "1977-01-01" @default.
• W2070291088 modified "2023-09-26" @default.
• W2070291088 title "Experimental difficulties in assaying a membrane-bound acyltransferase from rabbit mammary tissue" @default.
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• W2070291088 doi "https://doi.org/10.1016/0020-711x(77)90126-4" @default.
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