TY - JOUR
T1 - Purification and Partial Characterization of Fibrillin, a Cysteine-rich Structural Component of Connective Tissue Microfibrils
AU - Sakai, Lynn Y.
AU - Keene, Douglas R.
AU - Glanville, Robert W.
AU - Bachinger, Hans Peter
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1991
Y1 - 1991
N2 - Fibrillin, a connective tissue macromolecule (Mr = 350,000) which is normally insoluble in its tissue form, has been purified from the medium of human skin fibroblast and ligament cells in culture. Analysis of the amino acid composition indicates that fibrillin contains approximately 14% cysteine, of which one-third appears to be in the free reactive sulfhydryl form. Electron microscopic images of fibrillin reveal an extended, flexible molecule approximately 148 nm long and 2.2 nm wide. These length measurements are consistent with shape calculations based upon velocity sedimentation data. It is likely that the material we have purified from cell culture medium represents monomeric fibrillin consisting of a single polypeptide chain. Additional ultrastructural immunohistochemical data presented here suggest a model for the parallel, head-to-tail alignment of fibrillin molecules in microfibrils.
AB - Fibrillin, a connective tissue macromolecule (Mr = 350,000) which is normally insoluble in its tissue form, has been purified from the medium of human skin fibroblast and ligament cells in culture. Analysis of the amino acid composition indicates that fibrillin contains approximately 14% cysteine, of which one-third appears to be in the free reactive sulfhydryl form. Electron microscopic images of fibrillin reveal an extended, flexible molecule approximately 148 nm long and 2.2 nm wide. These length measurements are consistent with shape calculations based upon velocity sedimentation data. It is likely that the material we have purified from cell culture medium represents monomeric fibrillin consisting of a single polypeptide chain. Additional ultrastructural immunohistochemical data presented here suggest a model for the parallel, head-to-tail alignment of fibrillin molecules in microfibrils.
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M3 - Article
C2 - 1860873
AN - SCOPUS:0026315446
SN - 0021-9258
VL - 266
SP - 14763
EP - 14770
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 22
ER -