| First Author | Costell M | Year | 1996 |
| Journal | FEBS Lett | Volume | 396 |
| Issue | 2-3 | Pages | 127-31 |
| PubMed ID | 8914972 | Mgi Jnum | J:37186 |
| Mgi Id | MGI:84507 | Doi | 10.1016/0014-5793(96)01082-4 |
| Citation | Costell M, et al. (1996) Structural characterization of recombinant domain II of the basement membrane proteoglycan perlecan. FEBS Lett 396(2-3):127-31 |
| abstractText | Mouse perlecan domain II (325 residues), consisting of four cysteine-rich LA modules, one IG module and a link region, was obtained in purified form from a stably transfected mammalian cell clone. Rotary shadowing electron microscopy demonstrated a globular domain connected to a short rod-like segment of variable length. This suggested that tandem arrays of LA modules form rod-like elements. Folding into a native structure was indicated by the sharing of immunological epitopes with tissue perlecan, a CD spectrum demonstrating 37% beta structure and a limited susceptibility to proteolysis. The domain also showed N-glycosylation of a single acceptor site and 7-8 O-linked oligosaccharides. The latter were located mainly in the link region within proline-rich sequences. |
