Hydrolysis of the Lipoprotein Fractions of Milk by Phospholipase C

Phospholipase C hydrolyzed about 90% of the lipid phosphorus of both low- and high-density lipoprotein fractions of milk. Phosphatidyl choline, phosphatidyl ethanolamine and sphingomyelin were most readily hydrolyzed whereas phosphatidyl serine and inositol were only hydrolyzed after the other phosp...

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Bibliographic Details
Published in:Journal of dairy science 1972-04, Vol.55 (4), p.408-412
Main Authors: O’Mahony, J.P., Shipe, W.F.
Format: Article
Language:English
Subjects:
Animals
Cattle
Chromatography, Thin Layer
dairy products
Female
Hydrolysis
Lipoproteins - analysis
Methods
Milk - analysis
Phospholipases
Phospholipids - analysis
Phospholipids - metabolism
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Summary:Phospholipase C hydrolyzed about 90% of the lipid phosphorus of both low- and high-density lipoprotein fractions of milk. Phosphatidyl choline, phosphatidyl ethanolamine and sphingomyelin were most readily hydrolyzed whereas phosphatidyl serine and inositol were only hydrolyzed after the other phospholipids had been almost completely hydrolyzed. By contrast only about 60% of the native phospholipids in milk were hydrolyzed, indicating that some are protected. That phospholipase C inhibited oxidation indicated that the phospholipids available for hydrolysis were also oxidized.
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(72)85507-3