Journals / Turkish Journal of Botany / 2005 / Cilt: 29 - Sayı: 3
Purification and Partial Characterisation of an Acid Lipase in Germinating Lipidbody Linseedlings
- Journal
- Turkish Journal of Botany
- Pages
- 177–184
- DOI
- —
Abstract
Electrophoretic analysis of germinating linseed proteins showed a gradual decrease in the quantity of a protein with a molecular weight of 42 kDa. This protein accumulates after 36 h of germination in synchronisation with an increase in lipase activity, and a decrease in the quantity of the total lipids. The 42 kDa subunit was found to be a lipid body membrane protein. This protein was isolated and identified by immunoprecipitation as a subunit of lipase. The linseed lipase acted on a wide range of triacylglycerols and had optimal activity at pH 4.7. The activity of the enzyme was slightly affected by a high concentration of salts and EDTA, while high concentrations of non-ionic detergents exhibited a pronounced inhibitory effect. These data suggest that the isolated 42 kDa protein is most likely a linseed acid lipase responsible for the breakdown of lipids during germination.
Özet
Electrophoretic analysis of germinating linseed proteins showed a gradual decrease in the quantity of a protein with a molecular weight of 42 kDa. This protein accumulates after 36 h of germination in synchronisation with an increase in lipase activity, and a decrease in the quantity of the total lipids. The 42 kDa subunit was found to be a lipid body membrane protein. This protein was isolated and identified by immunoprecipitation as a subunit of lipase. The linseed lipase acted on a wide range of triacylglycerols and had optimal activity at pH 4.7. The activity of the enzyme was slightly affected by a high concentration of salts and EDTA, while high concentrations of non-ionic detergents exhibited a pronounced inhibitory effect. These data suggest that the isolated 42 kDa protein is most likely a linseed acid lipase responsible for the breakdown of lipids during germination.