作者: John D. Bartlett , James P. Simmer , Jun Xue , Henry C. Margolis , Edgard C. Moreno
DOI: 10.1016/S0378-1119(96)00525-2
关键词: Molecular biology 、 MMP20 、 Open reading frame 、 Collagenase 、 Molecular cloning 、 cDNA library 、 Northern blot 、 Biology 、 Complementary DNA 、 Enamel organ
摘要: A cDNA encoding a novel matrix metalloproteinase (MMP) was isolated from porcine enamel organ-specific library. Multiple tissue northern blot analysis revealed the presence of two mRNA transcripts which were expressed only in organ. The 1968 bp or 3420 length and resulted utilization alternative polyadenylation sites. open reading frame cloned encodes protein composed 483 amino acids. MMP has predicted molecular mass 54.1 kDa, is similar to that stromelysins collagenases, although it not member either these classes MMPs. motif does contain consensus hemopexin-like domain because lacks critical tryptophan proline residue at appropriate positions. Since new gene family its expression appears limited organ, we have named enamelysin.