TY - JOUR
T1 - Production of recombinant human tropoelastin
T2 - Characterization and demonstration of immunologic and chemotactic activity
AU - Indik, Zena
AU - Abrams, William R.
AU - Kucich, Umberto
AU - Gibson, Carolyn W.
AU - Mecham, Robert P.
AU - Rosenbloom, Joel
N1 - Funding Information:
i Supported by National Institutes of Health Research AR20553, National Foundation-March of Dimes Grant l-989, grant from the American Lung Association. ’ To whom correspondence should be addressed.
PY - 1990/7
Y1 - 1990/7
N2 - Tropoelastin cannot readily be prepared in quantity from natural sources and this has limited research in several important areas including structure/function relationships and fiber assembly. In order to eliminate this limitation, human tropoelastin has been expressed in a recombinant bacterial system and the protein has been highly purified. The size, amino acid composition, and sequence of the amino terminus of the recombinant tropoelastin (rTE) all agree with values predicted by the nucleotide sequence of the cDNA used in the expression vector. The rTE exhibits cross-reactivity with antibodies directed against a mixture of peptides derived from human elastin as well as antibody against a defined peptide located at the carboxy terminus of the protein. In addition, the rTE is chemotactic for fetal calf ligament fibroblasts. These results suggest that rTE could be a useful reagent for many types of studies.
AB - Tropoelastin cannot readily be prepared in quantity from natural sources and this has limited research in several important areas including structure/function relationships and fiber assembly. In order to eliminate this limitation, human tropoelastin has been expressed in a recombinant bacterial system and the protein has been highly purified. The size, amino acid composition, and sequence of the amino terminus of the recombinant tropoelastin (rTE) all agree with values predicted by the nucleotide sequence of the cDNA used in the expression vector. The rTE exhibits cross-reactivity with antibodies directed against a mixture of peptides derived from human elastin as well as antibody against a defined peptide located at the carboxy terminus of the protein. In addition, the rTE is chemotactic for fetal calf ligament fibroblasts. These results suggest that rTE could be a useful reagent for many types of studies.
UR - http://www.scopus.com/inward/record.url?scp=0025322996&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(90)90521-Y
DO - 10.1016/0003-9861(90)90521-Y
M3 - Article
C2 - 2191629
AN - SCOPUS:0025322996
SN - 0003-9861
VL - 280
SP - 80
EP - 86
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -