Tuberculosis Hospitalization

Patterson, Raymond S.

doi:10.2105/ajph.17.6.629-a

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“…HSPGs have been implicated in the deposition of amyloid in Alzheimer's disease [30,31] and the deposition of abnormal prion protein in scrapie infection and other prion diseases [32,33]. Recently, bovine spongiform encephalopathy (' BSE '), a prion-based infection associated with ' mad cow disease ', has been the source of increasing public concern [34,35]. In an effort to gain an improved understanding of bovine spongiform encephalopathy, our laboratory has undertaken to purify the major HSPG found in adult bovine brain tissue, identify its core protein and examine its HS GAG chains.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of heparan sulphate proteoglycan from bovine brain

PARK¹,

YU²,

GUNAY³

et al. 1999

Biochem. J.

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A heparan sulphate proteoglycan was purified from adult bovine brain tissues and its structure was characterized. The major heparan sulphate proteoglycan from whole bovine brain had a molecular mass of 200 kDa on denaturing SDS\PAGE and a core protein size of 66 kDa following the removal of glycosaminoglycan chains. Fractionation on DEAE-Sephacel showed that this proteoglycan consisted of three major forms having high, intermediate and low overall charge. All core proteins were identical in size and reacted with heparan sulphate proteoglycanstub antibody and an antibody made to a synthetic peptide based on rat glypican. The three forms of proteoglycans had identical peptide maps and their amino acid compositional analysis did not match any of the known glypicans. The internal sequence of a major peptide showed only 37.5 % sequence similarity with human glypican 5. The glycosaminoglycan chain sizes of the three forms of this proteoglycan, determined after β-elimination by

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Section: Introductionmentioning

confidence: 99%