Philip J Roeth

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Clusterin prepared from human serum by monoclonal antibody affinity chromatography was devoid of the ability to increase the rates of formation of insoluble immune complexes associated with clusterin preparations obtained by polyclonal IgG affinity chromatography. Clusterin did not bind to AMP-Sepharose but the protein responsible for increasing the rates(More)
Clusterin was purified from human serum by sequential affinity chromatography over IgG-, protein A- and Con A-Sepharose. The protein was approximately 70 kDa by SDS/PAGE under nonreducing conditions and was resolved into approximately 35 kDa bands under reducing conditions. The protein reacted with clusterin-specific Mabs in ELISA and in Western blots. Its(More)
BACKGROUND AND OBJECTIVES Currently, plasma fractionation involves multiple processing steps using established methods such as ethanol precipitation and column chromatography. The known limitations associated with conventional purification techniques, combined with strict regulations on safety and high demand for particular plasma proteins, have resulted in(More)
Treatment of anti-ovalbumin rabbit IgG with diethylpyrocarbonate (DEPC) at concentrations up to 100 microM led to a progressive decrease in the rates of formation of insoluble immune complexes, without affecting the final extent of immune complex formation. DEPC concentrations approximately 10-fold higher were needed to give comparable decreases in the(More)
The Gradiflow (Life Therapeutics, Frenchs Forest, Australia) system is a novel electrophoretic technique that uses the dual characteristics of size and charge to separate target macromolecules from complex biological solutions. The system has the potential to selectively remove a range of moieties from blood and plasma in an in vivo system such as(More)
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