1,721,183 research outputs found
Hunter syndrome: presence of material cross-reacting with antibodies against iduronate sulfatase
No full textPolyclonal antibodies were obtained from rabbits by injection of iduronate sulfatase purified 35,000-fold from human placenta, after elution of the enzyme from sodium dodecyl sulfate (SDS) polyacrylamide gels. The specificity of these antibodies towards iduronate sulfatase was demonstrated by immunoprecipitation of enzyme activity; the level of other lysosomal hydrolases and sulfatases remained constant. Immunoblot of iduronate sulfatase from various human sources showed that the antibody recognises a polypeptide of mol.wt. 72,000 daltons in placenta and serum, and a form of mol.wt. 60,000 daltons in fibroblasts. No immunoprecipitable peptide was found in urine or in the culture medium of fibroblasts. Polypeptides of the same molecular weight were recognised in serum and in fibroblasts of Hunter patients. The presence of altered proteins in these patients was also shown by competition experiments. The addition of Hunter proteins alters the binding of normal enzyme to the antibody. © 1987 Springer-Verlag
Iduronate sulfatase from human placenta
No full textThe major enzyme component of idunorate sulfatase from human placenta was purified 30 000-fold by a five-step procedure. Sucrose gradient centrifugation of the native enzyme gave a molecular weight estimate of 80 000 ± 10 000. Electrophoresis in sodium dodecyl sulfate of the enzyme reduced with mercaptoethanol showed a protein band of Mr 82 000. We suggest that the enzyme is composed of a single polypeptide chain of Mr 80 000-90 000. © 1985
Expression of the two iduronate-2-sulfatase cDNAs
No full textThe iduronate-2-sulfatase (IDS) is a lysosomal enzyme that acts on sulphate groups on C-2 positions of the iduronic acid residues of the mucopolysaccharides heparan sulphate and dermatan sulphate. Recently, we described in mouse two IDS mRNAs: the first or canonic (MTA16), highly homologous to the human counterpart, the second or novel (MTA13), completely divergent from the canonic in the 3' region. In this study, by reverse transcriptase polymerase chain reaction (RT-PCR) we analyzed the expression of the two mRNA transcripts for the IDS gene in murine tissues, in various human cell-lines and in cells from some Hunter patients
- …
