دورية أكاديمية
Biosynthesis of phosphatidic acid by glycerophosphate acyltransferases in rat liver mitochondria and microsomes.
العنوان: | Biosynthesis of phosphatidic acid by glycerophosphate acyltransferases in rat liver mitochondria and microsomes. |
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المؤلفون: | Mok AY; Department of Biochemistry, University of Western Ontario, London, Canada., McMurray WC |
المصدر: | Biochemistry and cell biology = Biochimie et biologie cellulaire [Biochem Cell Biol] 1990 Dec; Vol. 68 (12), pp. 1380-92. |
نوع المنشور: | Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: Canadian Science Publishing Country of Publication: Canada NLM ID: 8606068 Publication Model: Print Cited Medium: Print ISSN: 0829-8211 (Print) Linking ISSN: 08298211 NLM ISO Abbreviation: Biochem Cell Biol Subsets: MEDLINE |
أسماء مطبوعة: | Publication: 2011- : Ottawa, ON : Canadian Science Publishing Original Publication: Ottawa, Ont. : National Research Council of Canada, c1986- |
مواضيع طبية MeSH: | Glycerol-3-Phosphate O-Acyltransferase/*metabolism , Membrane Proteins/*metabolism , Microsomes, Liver/*enzymology , Mitochondria, Liver/*enzymology , Phosphatidic Acids/*biosynthesis, Acylation ; Animals ; Carnitine/analogs & derivatives ; Carnitine/metabolism ; Cations, Divalent/pharmacology ; Detergents/pharmacology ; Glycerol-3-Phosphate O-Acyltransferase/isolation & purification ; Glycerophosphates/metabolism ; Membrane Proteins/isolation & purification ; Palmitoyl Coenzyme A/metabolism ; Palmitoylcarnitine/metabolism ; Rats |
مستخلص: | The acyltransferases that catalyze the synthesis of phosphatidic acid from labelled sn-[14C]glycero-3-phosphate and fatty acyl carnitine or coenzyme A derivatives have been shown to be present in both isolated mitochondria and microsomes from rat liver. The major reaction product was phosphatidic acid in both subcellular fractions. A small quantity of lysophosphatidic acid and neutral lipids were produced as by-products. Divalent cations had significant effects on both mitochondrial and microsomal fractions in stimulating acylation using palmitoyl CoA, but not when palmitoyl carnitine was used as the acyl donor. Palmitoyl CoA and palmitoyl carnitine could be used for acylation by both mitochondria and microsomes. Mitochondria were more permeable to palmitoyl carnitine and readily used it as the substrate for acylation. On the other hand, microsomes yielded a better rate with palmitoyl CoA and the rate of acylation from palmitoyl carnitine in microsomes was correlated with the degree of mitochondrial contamination. The enzymes were partially purified from Triton X-100 extracts of subcellular fractions. Based on the differences of substrate utilization, products formed, divalent cation effects, molecular weights, and polarity, the mitochondrial and microsomal acyltransferases appeared to be different enzymes. |
المشرفين على المادة: | 0 (Cations, Divalent) 0 (Detergents) 0 (Glycerophosphates) 0 (Membrane Proteins) 0 (Phosphatidic Acids) 13962-05-5 (oleoylcarnitine) 1763-10-6 (Palmitoyl Coenzyme A) 1935-18-8 (Palmitoylcarnitine) EC 2.3.1.15 (Glycerol-3-Phosphate O-Acyltransferase) S7UI8SM58A (Carnitine) |
تواريخ الأحداث: | Date Created: 19901201 Date Completed: 19910523 Latest Revision: 20190912 |
رمز التحديث: | 20221213 |
DOI: | 10.1139/o90-201 |
PMID: | 2085434 |
قاعدة البيانات: | MEDLINE |
تدمد: | 0829-8211 |
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DOI: | 10.1139/o90-201 |