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Biotechnol Lett ; 27(9): 665-70, 2005 May.
Article in English | MEDLINE | ID: mdl-15977075

ABSTRACT

Using overlap elongation PCR, we created repetitive DNA libraries encoding the elastin VPGVG and collagen-like GERGDRGDP sequences. From these libraries we isolated two repetitive DNA sequences, Col-5 encoding [(GERGDRGDP)(5)GER], and Ela-16 encoding [(VPGVG)(16)VPG]. Both proteins were expressed as thioredoxin fusion proteins. The resulting recombinant extracellular matrix-like proteins had the expected properties (cell adhesive ability and thermally responsive structural change) of the functional motif sequence unit used.


Subject(s)
Biotechnology/methods , Collagen/chemistry , Elastin/chemistry , Extracellular Matrix/metabolism , Recombinant Proteins/chemistry , Amino Acid Motifs , Animals , Base Sequence , Cell Adhesion , DNA/chemistry , Electrophoresis, Agar Gel , Electrophoresis, Polyacrylamide Gel , Gene Library , Hot Temperature , Mice , Molecular Sequence Data , NIH 3T3 Cells , Oligonucleotides/chemistry , Polymerase Chain Reaction , Sequence Analysis, DNA , Temperature , Thioredoxins/chemistry
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