Apr 10, 1976

Kinetic study of the action of snake venom phospholipase A2 on human serum high density lipoprotein 3

The Journal of Biological Chemistry
N M PattnaikA M Scanu

Abstract

The hydrolysis of the phospholipids of intact human serum high density lipoprotein 3 (HDL3) by pure alpha-phospholipase A2 from Crotalus adamanteus was studied by pH-stat titration. The enzyme quantitatively hydrolyzed phosphatidylcholine and phosphatidylethanolamine and left sphinogomyelin intact, yielding a stable and water-soluble modified HDL. Lysophospholipids and free fatty acids, the products of hydrolysis, remained in the lipoprotein. When 1 mol of defatted bovine serum albumin/mol of substrate phospholipids was added to the reaction mixture, up to 60% of the fatty acids and 85% of the lysophospholipids were removed from the modified lipoprotein. The immunological reactivity of the hydrolyzed HDL remained unaltered in both the presence and absence of albumin. The changes in the physical properties of the lipoprotein during hydrolysis were rather small, the most notable being an increase in the hydrated density and in the electrophoretic mobility in alkaline buffers. The hydrolysis followed an apparent first order time course with product inhibition (KI) and yielded values of kcat/Km = 7 X 10(5 M(-1)s(-1) and KI congruent to 1 X 10(-4) M. Addition of albumin to the reaction mixture relieved the product inhibition without...Continue Reading

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Mentioned in this Paper

Buffers
Thermodynamics
Epicholesterol
Snake Venoms
Phospholipase A2, human
HDL-Cholesterol Subclass 3 Measurement
Hyrex Brand of Dimenhydrinate
Huntington DISEASE-LIKE 3 (Disorder)
ALB
Lysophospholipids

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