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Lipoprotein lipase of goat mammary tissue: comparison of extraction methods

Published online by Cambridge University Press:  01 June 2009

Yves Chilliard
Affiliation:
Animal Science Department Research Laboratory, INRA Institut National Agronomique Paris-Grignon, 16, rue Claude Bernard – 75231 Paris Cedex 05, France

Summary

Mammary lipoprotein lipase of lactating goats was extracted by 3 methods: homogenization of tissue acetone-ether powders; aqueous homogenization of crude tissue using an Ultra-Turrax apparatus; aqueous homogenization of crude tissue using a Sorvall Omni-mixer microhomogenizer. Although there were differences between absolute values obtained by the 3 methods, each type of homogenate had a lipolytic activity with lipoprotein lipase characteristics (i.e. more than 90% inhibition by serum omission or NaCl addition). Furthermore, the 3 methods were highly correlated and presented similar variations with the stage of lactation, in parallel with long-chain fatty acid secretion into milk. Repeatability of the measure of homogenate lipolytic activities was about 8%, whereas day-to-day repeatability of enzyme extraction and assay was about 20% for each method.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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