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Neutralizing monoclonal antibodies were derived to human rotaviruses RV-4 (serotype 1), RV-5 (serotype 2), and ST-3 (serotype 4). By enzyme immunoassay and fluorescent focus neutralization, eight of the antibodies appeared to be specific for the immunizing serotype, and so have potential as reagents for rotavirus serotyping by enzyme immunoassay. Seven of(More)
PH8 monoclonal antibody has previously been shown to react with all three aromatic amino acid hydroxylases, being particularly useful for immunohistochemical staining of brain tissue [Haan, Jennings, Cuello, Nakata, Chow, Kushinsky, Brittingham & Cotton (1987) Brain Res. 426, 19-27]. Western-blot analysis of liver extracts showed that PH8 reacted with(More)
Deficiency of human dihydropteridine reductase (hDHPR) causes malignant hyperphenylalaninemia. We report the isolation of a cDNA clone for hDHPR that spans the complete coding region, and present the nucleotide sequence and the predicted amino acid sequence. The hDHPR protein does not share extensive homology with the enzymatically related protein human(More)
Two-dimensional gel electrophoresis of immunopurified monkey liver phenylalanine hydroxylase showed a novel form of the enzyme, in 4 out of 24 monkeys, in which each polypeptide spot was split into a doublet with the same charge but slightly different mobility in the sodium dodecyl sulphate/polyacrylamide-gel-electrophoresis (as opposed to the(More)
Two-dimensional polyacrylamide gel analyses of purified human and monkey liver phenylalanine hydroxylase reveal that the enzyme consists of two different apparent molecular weight forms of polypeptide, designated H (Mr = 50,000) and L (Mr = 49,000), each containing three isoelectric forms. The two apparent molecular weight forms, H and L, represent the(More)
High performance liquid chromatography maps of tryptic and chymotryptic peptides from the W and L forms of rat phenylalanine hydroxylase differed by one peptide. Sequencing of the variant tryptic peptides showed a substitution of threonine in the W form by isoleucine in the L form and this same difference was confirmed in the chymotryptic peptides. This(More)
Monoclonal antibody PH7 has specificity for the phosphorylated form of the human liver phenylalanine hydroxylase and negligible reactivity towards the dephosphorylated form of the native enzyme by enzyme-linked immunoassay. PH7 binds specifically to the phosphorylated form of the liver enzyme after SDS/polyacrylamide-gel electrophoresis and transfer to(More)
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