Abstract
Publisher Summary Acylglycerone-phosphate reductase—a membrane-bound enzyme present in animal tissues—catalyzes the reduction of long-chain acyldihydroxyacetone phosphate (acyI-DHAP) or long-chain alkyl-DHAP by NADPH to the corresponding sn -glycerol 3-phosphate derivatives. In liver and other organs, the major fraction of the enzyme is present in peroxisomes. The enzyme has been solubilized and partially purified from Ehrlich ascites cell microsomes and purified to homogeneity from guinea pig liver peroxisomes. This chapter describes a method for the preparation of the homogeneous enzyme from guinea pig liver peroxisomes. The enzyme activity is assayed by measuring the radioactive lipid product formed after incubating alkyl-DHAP with B-[4- 3 H] NADPH. The purification of alkyldihydroxyacetone phosphate is discussed in the chapter. On sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, the purified enzyme shows a single protein band of relative mobility corresponding to 60,000 molecular weight. On gel filtration, in the presence of octylglucoside, the molecular weight of the enzyme is estimated at 75,000. The enzyme has a broad pH optimum between pH 6.5 and 7.5.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
