Effect of phospholipase A2 digestion on the conformation and lysine/fibrinogen binding properties of human lipoprotein[a]

Effect of phospholipase A2 digestion on the conformation and lysine/fibrinogen binding properties of human lipoprotein[a]

In vitro hydrolysis of human lipoprotein[a] (Lp[a]) by phospholipase A2 (PLA2) decreased the phosphatidylcholine (PC) content by 85%, but increased nonesterified fatty acids 3.2-fold and lysoPC 12.9-fold. PLA2-treated Lp[a] had a decreased molecular weight, increased density, and greater electronega...

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Bibliographic Details
Main Authors: Gunther M. Fless, Elliot W. Kirk, Olga Klezovitch, José Y. Santiago, Celina Edelstein, Jane Hoover-Plow, Angelo M. Scanu
Format: Article
Language:English
Published: Elsevier 1999-04-01
Series:Journal of Lipid Research
Subjects:
Lp[a] structure
apo[a]
apoB
lysine binding sites
phosphatidylcholine
lysophosphatidylcholine
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520321374

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http://www.sciencedirect.com/science/article/pii/S0022227520321374

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