Document Detail


Isolation and characterization of cytidine diphosphate diglyceride from beef liver.
MedLine Citation:
PMID:  169258     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cytidine diphosphate diglyceride was isolated from beef liver by a combination of silicic acid column, DEAE-cellulose column, and this layer chromatography. The product (5.8 to 17.4 mumol/kg of liver) contained cytidine/phosphate/fatty acids in the molar proportions 1.05/2.0/2.05 (theoretical, 1.0/2.0/2.0) (average for three preparations). The liponucleotide was split quantitatively by a partially purified hydrolase from Escherichia coli, specific for CDP-diglyceride, (Raetz, C. R. H., Hirschberg, C. B., Dowhan, W., Wickner, W. T., and Kennedy, E. P. (1972) J. Biol. Chem. 247, 2245-2247) into phosphatidic acid and a water-soluble nucleotide that was chromatographically identical with CMP. No dCMP was located in these hydrolysates. The liver liponucleotide was more effective than a synthetic preparation of CDP-diglyceride in promoting the formation of phosphatidylinositol with guinea pig brain microsomes. The fatty acid composition of CDP-diglyceride was compared with metabolically related phospholipids from beef liver. The liponucleotide had a similar composition to phosphatidylinositol, characterized by a high level of stearate and with arachidonate as the major unsaturated fatty acid. The content of arachidonate in both lipids was significantly higher than that in phosphatidic acid. The profile of fatty acids of cardiolipin was quite unlike that of CDP-diglyceride. These findings suggest several alternatives for the metabolic origins of beef liver CDP-diglyceride: (a) CDP-diglyceride is formed from an atypical pool of phosphatidic acid, (b) the enzyme is selective for arachidonoyl-containing species of phosphatidic acid, (c) the liponucleotide may also be derived from phosphatidylinositol by the back-reaction of CDP-diglyceride: inositol phosphatidyltransferase.
Authors:
W Thompson; G MacDonald
Related Documents :
7397208 - Galactolipid synthesis in vicia faba leaves. v. redistribution of 14c-labelling in the ...
3086318 - Remodeling of arachidonate-containing phosphoglycerides within the human neutrophil.
6192808 - Phosphatidic acid and phosphatidylinositol labelling in adipose tissue. the role of end...
10486148 - Phase properties of liquid-crystalline phosphatidylcholine/phosphatidylethanolamine bil...
14456208 - Alterations in the permeability of neurospora crassa due to polyene antibiotics.
15117068 - Optimizing the determination of haloacetic acids in drinking waters.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  250     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1975 Sep 
Date Detail:
Created Date:  1975-12-04     Completed Date:  1975-12-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  6779-85     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Brain / enzymology
Cardiolipins
Cattle
Cytidine Diphosphate Diglycerides* / analysis,  isolation & purification
Escherichia coli
Fatty Acids / analysis
Guinea Pigs
Liver / analysis*
Nucleoside Diphosphate Sugars*
Phosphatidic Acids / analysis
Phosphatidylinositols
Phosphoric Monoester Hydrolases
Phosphotransferases / metabolism
Chemical
Reg. No./Substance:
0/Cardiolipins; 0/Cytidine Diphosphate Diglycerides; 0/Fatty Acids; 0/Nucleoside Diphosphate Sugars; 0/Phosphatidic Acids; 0/Phosphatidylinositols; EC 2.7.-/Phosphotransferases; EC 3.1.3.-/Phosphoric Monoester Hydrolases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Pulmonary angiotensin-converting enzyme. Structural and catalytic properties.
Next Document:  Human phosphoribosylpyrophosphate synthetase. Comparison of purified normal and mutant enzymes.