Subcellular fractions of rat liver were isolated by density-gradient centrifugation on a linear Metrizamide gradient and were assayed for marker enzymes of peroxisomes, lysosomes, microsomes and mitochondria. Alkylglyceronephosphate synthase catalysing the formation of the ether bond in glycerolipids was also determined along the gradient. The enzyme was found to be enriched in the peroxisomal and the microsomal fractions thus, displaying a bimodal distribution pattern. Two reaction-products each, alkylglycerone phosphate and alkylglycerone were obtained in the enzymic assays performed, the ratio of which was clearly dependent upon the fraction employed. Alkylglycerone phosphate was mainly synthesized by the 'peroxisomal synthase', whereas an inverse proportion was observed assaying the microsomal counterpart. Furthermore, comparing the mean specific activities of both the enzymes the microsomal one was shown to be roughly twice as active in metabolizing 1-0-palmitoylglycerone 3-phosphate, simultaneously displaying a somewhat different sensitivity to NaF. These findings provide a first line of evidence, that two separate synthases, one in microsomes and another one in peroxisomes might be engaged in the biosynthesis of 1-0-alkylglycerolipids in rat liver.
Subzelluläre Verteilung der AlkyIglyceronphosphat-Synthase in der RattenleberZusammenfassung: Mittels Dichtegradientenzentrifugation unter Verwendung linearer Metrizamid-Gradienten wurden aus Rattenleber subzelluläre Fraktionen gewonnen. Neben Leitenzymen für Peroxisomen, Lysosomen, Mikrosomen und Mitochondrien wurde in den einzelnen Gradientenfraktionen auch Alkylglyceronphosphat-Synthase bestimmt. Die Synthase katalysiert im Rahmen der Biosynthese von sogenannten Etherlipiden die Substitution eines langkettigen Acylrestes durch einen Fettalkohol.