@inbook{24acc8cdd5c74fff8034185f14896049,
title = "Elastin purification and solubilization",
abstract = "The functional form of elastin is a highly cross-linked polymer that organizes as sheets or fibers in the extracellular matrix. Purification of the mature protein is problematic because its insolubility precludes its isolation using standard wet-chemistry techniques. Instead, relatively harsh experimental approaches designed to remove nonelastin “contaminates” are employed to generate an insoluble product that has the amino acid composition expected of elastin. Although soluble, tropoelastin also presents problems for isolation and purification. The protein's extreme stickiness and susceptibility to proteolysis require careful attention during purification and in tropoelastin-based assays. This chapter describes the most common approaches for purification of elastin and for preparing solubilized forms of the protein.",
keywords = "Cross-links, Desmosine, Elastic fiber, Elastin, Microfibril",
author = "Halabi, {Carmen M.} and Mecham, {Robert P.}",
note = "Funding Information: Original work discussed in this report was supported by NIH Grants HL53325 and HL105314. C.M.H. is a Scholar of the Child Health Research Center at Washington University School of Medicine, NIH K12-HD076224. She also received support from NIH K08 HL135400, training Grant T32-HD043010-11, and the Mallinckrodt Foundation Physician-Scientist Training Program Fellow support. Publisher Copyright: {\textcopyright} 2018 Elsevier Inc.",
year = "2018",
doi = "10.1016/bs.mcb.2017.08.012",
language = "English",
series = "Methods in Cell Biology",
publisher = "Academic Press Inc.",
pages = "207--222",
booktitle = "Methods in Cell Biology",
}