Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 3 of 3
Full-Text Articles in Organisms
Sera Of Iga Nephropathy Patients Contain A Heterogeneous Population Of Relatively Cationic Alpha-Heavy Chains, Onn Haji Hashim
Sera Of Iga Nephropathy Patients Contain A Heterogeneous Population Of Relatively Cationic Alpha-Heavy Chains, Onn Haji Hashim
Onn Haji Hashim
Sera of IgA nephropathy (IgAN) patients and normal subjects were analysed by two-dimensional (2-D) gel electrophoresis. Densitometric analysis of the 2-D gels of IgAN patients and normal subjects revealed that their protein maps were comparable. There was no shift of pI values in the major alpha-heavy chain spots. However, the volume of the alpha-heavy chain bands were differently distributed. Distribution was significantly lower at the anionic region in IgAN patients (mean anionic:cationic ratio of 1.184 +/- 0.311) as compared to normal healthy controls (mean anionic:cationic ratio of 2.139 +/- 0.538). Our data are in support of the previously reported findings …
Galactose-Binding Lectin From The Seeds Of Champedak (Artocarpus Integer): Sequences Of Its Subunits And Interactions With Human Serum O-Glycosylated Glycoproteins, Onn Haji Hashim
Onn Haji Hashim
Our group has previously reported the isolation, partial characterisation, and application of a Galbeta1-3GalNAc- and IgA1-reactive lectin from the seeds of champedak (Artocarpus integer). In the present study, we have subjected the purified lectin to reverse-phase high performance liquid chromatography and sequenced its subunits. Determination of the N-terminal sequence of the first 47 residues of the large subunit demonstrated at least 95% homology to the N-terminal sequence of the alpha chains of a few other galactose-binding Artocarpus lectins, The two smaller subunits of the lectin, each comprised of 21 amino acid residues, demonstrated minor sequence variability. Their sequences were generally …
Isolation Of A Mannose-Binding And Ige- And Igm-Reactive Lectin From The Seeds Of Artocarpus Integer, Onn Haji Hashim
Isolation Of A Mannose-Binding And Ige- And Igm-Reactive Lectin From The Seeds Of Artocarpus Integer, Onn Haji Hashim
Onn Haji Hashim
A mannose-binding lectin, termed champedak lectin-M, was isolated from an extract of the crude seeds of champedak (Artocarpus integer). On gel filtration chromatography, the lectin eluted in a single peak at elution volumes corresponding to 64 kDa, SDS-PAGE showed the mannose-binding lectin to be composed of 16.8 kDa polypeptides with some of the polypeptides being disulphide-linked to give dimers. When tested with all isotypes of immunoglobulins, champedak lectin-M demonstrated a selective strong interaction with human IgE and IgM, and a weak interaction with IgA2, The binding interactions of lectin-M were metal ion independent. The lectin was also shown to interact …