Shin‐Ichiro Nishimura

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTChemospecific manipulations of a rigid polysaccharide: syntheses of novel chitosan derivatives with excellent solubility in common organic solvents by regioselective chemical modificationsShinichiro Nishimura, Osamu Kohgo, Keisuke Kurita, and Hiroyoshi KuzuharaCite this: Macromolecules 1991, 24, 17, 4745–4748Publication Date (Print):August 1, 1991Publication History Published online1 May 2002Published inissue 1 August 1991https://pubs.acs.org/doi/10.10

Common oligosaccharides and aldehyde-attached glycoproteins derived from enzymatic modifications can be captured by glycoblotting based on oxylamino-containing polymers. The combination of this glycoblotting and MALDI-TOF/TOF mass spectrometry enabled a high-throughput analytical method to be developed. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2005/z461685_s.pdf or from the author. Please note: The publisher is not responsible

Global glycomics of human whole serum glycoproteins appears to be an innovative and comprehensive approach to identify surrogate non-invasive biomarkers for various diseases. Despite the fact that quantitative glycomics is premised on highly efficient and reproducible oligosaccharide liberation from human serum glycoproteins, it should be noted that there is no validated protocol for which deglycosylation efficiency is proven to be quantitative. To establish a standard procedure to evaluate N-gl

A rapid and quantitative method for solid-phase methyl esterification of carboxy groups of various sialylated oligosaccharides has been established. The method employed a triazene derivative, 3-methyl-1-p-tolyltriazene, for facile derivatization of oligosaccharides immobilized onto general solid supports such as Affi-Gel Hz and gold colloidal nanoparticles in a multiwell plate. The workflow protocol was optimized for the solid-phase processing of captured sialylated/unsialylated oligosaccharides

Despite recent advances in our understanding of the significance of the protein glycosylation, the throughput of protein glycosylation analysis is still too low to be applied to the exhaustive glycoproteomic analysis. Aiming to elucidate the N-glycosylation of murine epidermis and dermis glycoproteins, here we used a novel approach for focused proteomics. A gross N-glycan profiling (glycomics) of epidermis and dermis was first elucidated both qualitatively and quantitatively upon N-glycan deriva

We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results. (i) Haptoglobin level was enhanced significantly in sera of prostate cancer. (ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan. The N-linked glycans at N184 were exclusively bi-antennary, and showed no di

The agreement between 4D-CE-MRA and DSA findings was good to excellent with respect to the fistula site and venous drainage.

Blocking flu: A cyclic peptide, cyclo(Ser-Gly-Gly-Gln-Ser-His-Asp)3, is an excellent scaffold for the synthesis of a cyclic glycopeptide carrying GM3 oligosaccharides with a potent inhibitory effect on the hemagglutination induced by the influenza virus. Tridentate binding of the gylcopeptide is shown to produce a much greater inhibitory effect than di- or monodentate binding. The shape of the glycopeptide protein scaffold, which is determined by the amino acid sequence employed, is also found t

Despite increasing importance of protein glycosylation, most of the large-scale glycoproteomics have been limited to profiling the sites of N-glycosylation. However, in-depth knowledge of protein glycosylation to uncover functions and their clinical applications requires quantitative glycoproteomics eliciting both peptide and glycan sequences concurrently. Here we describe a novel strategy for the multiplexed quantitative mouse serum glycoproteomics based on a specific chemical ligation, namely,