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- W2068770170 abstract "Abstract The effects of octylglucoside on the substrate specificity, kinetics and aggregation state of purified carnitine palmitoyltrasferase (CPT) from beef heart mitochondria were investigated and compared to the effects of Triton X‐100. Conditions in which CPT can be assayed in the absence of micelles and albumin, thereby eliminating miceller effects on the kinetic parameters, are described. When octylglucoside is substituted for Triton X‐100, the specificity of CPT in the forward direction shifts towards the long‐chain acyl‐CoAs, and large changes in the kinetic constants are observed. The K 0.5 for L‐carnitine varied as much as 50‐fold, depending on the acyl‐CoA and detergent used. At pH 8.0 and 200 μM palmitoyl‐CoA, the K 0.5 for L‐carnitine is 4.9 mM in 12 mM octylglucoside and 0.2 mM in 0.1% Triton X‐100. Octylglucoside enhances the activity of CPT with long‐chain acyl‐CoA and lowers the K 0.5 for these substrates. At pH 6.0, the K 0.5 for palmitoyl‐CoA is 24.2 μM in 0.1% Triton X‐100, in contrast to 3.1 μM in 12 mM octylglucoside. Octylglucoside is a competitive inhibitor of CPT with octanoyl‐CoA as substrate with a K i of 15 mM. Nonlinear kinetics for both acyl‐CoAs and L‐carnitine are observed when the concentration of octylglucoside is reduced to less than half of its critical micellar concentration (cmc). Gel filtration of CPT in octylglucoside below its cmc gives a single protein peak with a molecular mass of ca. 660,000 daltons. These data indicate that the catalytically active form of purified CPT is an aggregate that has quaternary structure and must have a very flexible catalytic site whose affinity for substrate and catalytic efficiency can be altered greatly by changes in environment and experimental conditions." @default.
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- W2068770170 date "1988-02-01" @default.
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- W2068770170 title "Effects of octylglucoside and triton X-100 on the kinetics and specificity of carnitine palmitoyltransferase" @default.
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- W2068770170 doi "https://doi.org/10.1007/bf02535291" @default.
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