Artigo Acesso aberto Revisado por pares

Positional Specificity of Lipoprotein Lipase

1972; Elsevier BV; Volume: 247; Issue: 20 Linguagem: Inglês

10.1016/s0021-9258(19)44705-4

ISSN

1083-351X

Autores

Nina H. Morley, A. Kuksis,

Tópico(s)

Muscle metabolism and nutrition

Resumo

Abstract The stereochemical course of hydrolysis of radioactive triolein was determined using lipoprotein lipase of cow's milk and rat postheparin plasma. [3H]Glycerol trioleate or glycerol [1-14C]trioleate was emulsified with total egg yolk lipids to provide 0.2 to 2.5 µCi of 3H or 0.03 µCi of 14C per µm substrate. The hydrolysis products were isolated at 1 to 45 min and free fatty acids and the various positional isomers of mono- and diglycerides were resolved by thin layer chromatography. In a total yield of 0.03 to 0.16 µmole of diglyceride, 9 to 30% was 1,3- and 70 to 91%, 1,2-(2,3-)diglyceride. The 2,3-isomer was 73 to 96% of the latter. The yield of free fatty acids and monoglycerides varied with the length of incubation. In 15 of 17 determinations, the 1-(3-)isomer accounted for 51 to 87% of the monoglyceride. It is suggested that lipoprotein lipase attacks preferentially position 1 in sn-glycerides and follows it by hydrolysis of the positions 2 and 3. An intermediate formation of 2,3-diglycerides during lipoprotein lipase hydrolysis may be important in avoiding stimulation of triglyceride and phospholipid biosynthesis which proceed via 1,2-diglycerides.

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