Distribution of distinct arachidonoyl-specific and non-specific isoenzymes of diacylglycerol kinase in baboon (Papio cynocephalus) tissues
Autor: | W C King, J A Glomset, R N Lemaitre, M L MacDonald |
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Rok vydání: | 1990 |
Předmět: |
Male
Diacylglycerol Kinase Phosphatidic Acids Biology Kidney Biochemistry Isozyme Substrate Specificity Diglycerides chemistry.chemical_compound biology.animal Testis Animals Tissue Distribution Molecular Biology Diacylglycerol kinase chemistry.chemical_classification Octyl glucoside Kinase Muscles Phosphotransferases Fatty acid Brain Cell Biology Phosphatidic acid Isoenzymes Enzyme chemistry Liver lipids (amino acids peptides and proteins) Spleen Baboon Papio Research Article |
Zdroj: | The Biochemical journal. 266(1) |
ISSN: | 0264-6021 |
Popis: | We investigated the diacyglycerol kinase species present in several baboon tissues using the substrates sn-1-stearoyl-2-arachidonoyl diacylglycerol and sn-1,2-didecanoyl diacylglycerol. Chromatography of octyl glucoside extracts of the baboon (Papio cynocephalus papio) tissues on hydroxyapatite columns revealed the presence of three diacylglycerol kinase species with different substrate preferences. One species markedly ‘preferred’ the substrate sn-1-stearoyl-2-arachidonoylglycerol, the two other species preferred sn-1,2-didecanoylglycerol. Measurement of the activity of the baboon brain diacylglycerol kinases toward diacylglycerols with a range of different fatty acid chains revealed a strict preference of the arachidonoyl diacylglycerol kinase for sn-1-acyl-2-arachidonoyl diacylglycerol, whereas the other enzymes showed no preference toward several long-chain-fatty-acid-containing diacylglycerols. The arachidonoyl diacylglycerol kinase was particularly abundant in brain and testis, whereas liver was practically devoid of this enzyme. The arachidonoyl diacylglycerol kinase from baboon brain was found to be predominantly associated with the particulate fraction and exhibited an apparent molecular mass of 130 kDa. |
Databáze: | OpenAIRE |
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