TROPOELASTIN HETEROGENEITY - IMPLICATIONS FOR PROTEIN FUNCTION AND DISEASE
TROPOELASTIN HETEROGENEITY - IMPLICATIONS FOR PROTEIN FUNCTION AND DISEASE
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DOI:
10.1165/ajrcmb/2.5.399
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发表时间:
1990-05-01
影响因子:
6.4
通讯作者:
DEAK, SB
中科院分区:
文献类型:
--
作者:
PARKS, WC;DEAK, SB
Elastic fibers are comprised of two components that are morphologically and chemically distinct. Most of the mature fiber (> 90%) is amorphous elastin, theinsoluble product of crosslinked tropoelastin monomers. Tropoelastin is rich in nonpolar amino acids, such as alanine, valine, and proline and the uncharged amino acid glycine. This amino acid composition results in hydrophobic interactions which are necessary for the elastic property of the fiber (3). Microfibrils, the other component of elastic fibers, are a complex of glycoproteins organized as small, 10-to 12-nm-diameter fibrils (4, 5). Microfibrils contain many charged and basic amino acid residues as well as numerous cysteines. This difference in