@article{fd08e230715f4470b6ae1f02113d2ed2,
title = "Quarternary structure and enzymological properties of the different hormone-sensitive lipase (HSL) isoforms",
abstract = "Hormone-sensitive lipase (HSL) is a key enzyme in the mobilization of energy in the form of fatty acids from intracellular stores of neutral lipids. The enzyme has been shown to exist in different isoforms with different molecular masses (84 kDa, 89 kDa and 117 kDa) expressed in a tissue-dependent manner, where the predominant 84 kDa form in adipocytes is the most extensively studied.",
keywords = "Base Sequence, Blotting, Western, Cold Temperature, Cyclic AMP-Dependent Protein Kinases, DNA Primers, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Isoenzymes, Microscopy, Electron, Transmission, Phosphorylation, Polymerase Chain Reaction, Protein Structure, Quaternary, Sterol Esterase",
author = "Christian Krintel and Cecilia Klint and H{\aa}kan Lindvall and Matthias M{\"o}rgelin and Cecilia Holm",
year = "2010",
doi = "10.1371/journal.pone.0011193",
language = "English",
volume = "5",
pages = "e11193",
journal = "PLOS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "6",
}