Methods for producing pure perlecan and other heparan...

Details Methods for producing pure perlecan and other heparan... Methods for producing pure perlecan and other heparan...

2006-08-22

2006-08-22

Riley, Jezia (Department: 1637)

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Preparing compound containing saccharide radical

C435S084000, C435S101000, C435S130000, C435S325000, C530S300000, C530S305000, C530S322000, C530S336000, C530S344000, C530S350000, C530S354000, C530S355000, C530S356000, C530S357000

Reexamination Certificate

active

07094580

ABSTRACT:
A method of perlecan isolation (from the EHS tumor) which produces “clean” (i.e. substantially “pure”) perlecan is disclosed. Clean perlecan is thus produced in sufficient quantities for use in a number of different in vitro and in vivo assays. In addition, this isolation method exploits a newly discovered aggregating property of a˜220 kDa heparan sulfate proteoglycan (HSPG) observed during gel filtration chromatography, which allows it to be effectively separated from non-aggregating perlecan. The method employs specific cation exchange, anion exchange, molecular sieve chromatography and immobilized GAG affinity chromatography. It is demonstrated that there are no other contaminating proteins in the perlecan and HSPG preparations, and that the perlecan core protein is intact. Improved, clean perlecan based, rodent models of fibrillar amyloid protein deposition, accumulation and/or persistence in tissues are disclosed.

REFERENCES:
Castillo et al. J. Biochem. 120, 433-444, 1996.
Yurchenco et al. Methods of Enzymology, vol. 245, pp. 489-518, 1994.
Rip et al. Biochem. J. vol. 288, pp. 1005-1010, 1992.
Oda et al. “Purification and characterization of perlecan fragment in urine of end-stage renal failure patients” Clinica Chimica Acta 255 (1996) 119-132.

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