Structural characterization of recombinant domain II of the basement membrane proteoglycan perlecan

FEBS Letters

Mann, Karlheinz²  Sasaki, Takako²  Yamada, Yoshihiko¹  Costell, Mercedes²  Timpl, Rupert² 

[1] National Institute of Dental Research, NIH, Bethesda, MD 20892, USA;Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany

关键词: Basement membrane;    Proteoglycan;    Recombinant protein;    Rod-like structure;   

DOI  :  10.1016/0014-5793(96)01082-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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% β 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.

【 授权许可】

Unknown