Novel self-association fibronectin sites.
In this study, we report a strong interaction between two contiguous proteolytic fragments of fibronectin, each having a mass of about 16 kDa. This interaction was stable in 4 M NaCl and 4 M urea and dissociation of the two fragments required buffers containing 0.5% sodium dodecyl sulphate. After purification, these peptides maintained their ability to interact when mixed. One fragment was made up of type III repeat 4 and part of 5, the other by repeat 6 and part of 5. Such strong interaction between two fibronectin regions may play a role in fibronectin conformation as well as during fibronectin fibril formation.
Carnemolla
B
B
Laboratory of Cell Biology, Istituto Nazionale per la Ricerca sul Cancro, Genoa, Italy.
Leprini
A
A
Querzé
G
G
Urbini
S
S
Zardi
L
L
D001483:Base Sequence; D001665:Binding Sites; D004355:Drug Stability; D005353:Fibronectins / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D012965:Sodium Chloride; D013820:Thermolysin / Q000378:metabolism; D014508:Urea
D005353:Fibronectins; D010446:Peptide Fragments; D011994:Recombinant Proteins; D012965:Sodium Chloride; D014508:Urea; D013820:Thermolysin