» Articles » PMID: 8224360

Purification and Characterization of Lipoprotein Lipase from the White Adipose, Skeletal Muscle, Cardiac Muscle, Mammary Gland and Lung Tissues of the Rat

Overview
Journal Int J Biochem
Specialty Biochemistry
Date 1993 Oct 1
PMID 8224360
Citations 3
Authors
Affiliations
Soon will be listed here.
Abstract

1. Lipoprotein lipase (LPL) was isolated from five rat tissues: white adipose, skeletal muscle, cardiac muscle, mammary gland and lung. 2. Specific activity of the preparations varied from 75 U/mg for skeletal muscle and 720 U/mg for adipose. 3. The preparations were further analysed using SDS-PAGE and a single component identified. The mol. wt of 61,000 Da of this component was consistent for all five of the tissue sources. 4. Significant differences in the values of the isoelectric points of the enzyme species were revealed. The values varied from 7.23 (SEM 0.022) for cardiac and lung to 7.51 (SEM 0.037) for mammary. 5. Two-dimensional electrophoresis, using isoelectric focusing in the first dimension and SDS-PAGE in the second revealed differences in the patterns of stained material derived from the five tissue sources.

Citing Articles

The response to fasting and refeeding reveals functional regulation of lipoprotein lipase proteoforms.

Carulla P, Badia-Villanueva M, Civit S, Carrascal M, Abian J, Ricart-Jane D Front Physiol. 2023; 14:1271149.

PMID: 37916217 PMC: 10617031. DOI: 10.3389/fphys.2023.1271149.


Purified chickpea or lentil proteins impair VLDL metabolism and lipoprotein lipase activity in epididymal fat, but not in muscle, compared to casein, in growing rats.

Boualga A, Prost J, Taleb-Senouci D, Krouf D, Kharoubi O, Lamri-Senhadji M Eur J Nutr. 2009; 48(3):162-9.

PMID: 19165521 DOI: 10.1007/s00394-009-0777-4.


Distinct immunoreactivities suggest the existence of potential tissue variants in rat lipoprotein lipase.

Soteriou A, Cryer A Biochem J. 1994; 299 ( Pt 2):417-23.

PMID: 8172602 PMC: 1138288. DOI: 10.1042/bj2990417.