Výsledky vyhledávání

Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry

Autor: T Y, Yen, R K, Joshi, H, Yan, N O, Seto, M M, Palcic, B A, Macher

Publikováno v: Journal of mass spectrometry : JMS. 35(8)

Cysteine residues and disulfide bonds are important for protein structure and function. We have developed a simple and sensitive method for determining the presence of free cysteine (Cys) residues and disulfide bonded Cys residues in proteins (100 pm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0d37a7a1f42ff7af3e951d0104117501
https://pubmed.ncbi.nlm.nih.gov/10972999

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Synthesis of the acceptor analog alphaFuc(1--2)alphaGal-O(CH2)7 CH3: a probe for the kinetic mechanism of recombinant human blood group B glycosyltransferase

Autor: V P, Kamath, N O, Seto, C A, Compston, O, Hindsgaul, M M, Palcic

Publikováno v: Glycoconjugate journal. 16(10)

We report the chemical synthesis of alphaFuc(1--2)alphaGal-O(CH2)7CH3 (1) an analog of the natural blood group (O)H disaccharide alphaFuc(1--2)betaGal-OR. Compound 1 was a good substrate for recombinant blood group B glycosyltransferase (GTB) and was

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1f5bcc944bbfab69adc615cb0156ab41
https://pubmed.ncbi.nlm.nih.gov/10972138

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Genetically tagged putative differentiation intermediates derived from undifferentiated HT29 human colon carcinoma cells

Autor: N O, Seto, V L, Seligy

Publikováno v: Cellular and molecular biology (Noisy-le-Grand, France). 45(2)

The HT29 colonic carcinoma cell line has proven to be a very practical tool for modelling aspects of colonic cell differentiation and toxification by chemotherapeutic agents. As an approach to subclone and clarify molecular events involved in subline

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1fb188d172740a00ef654096cd3c4b95
https://pubmed.ncbi.nlm.nih.gov/10230729

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Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli

Autor: N O, Seto, C A, Compston, S V, Evans, D R, Bundle, S A, Narang, M M, Palcic

Publikováno v: European journal of biochemistry. 259(3)

The human blood group A and B glycosyltransferases catalyze the transfer of GalNAc and Gal, to the (O)H-precursor structure Fuc alpha (1-2)Gal beta-OR to form the blood group A and B antigens, respectively. Changing four amino acids (176, 235, 266 an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::043fdc4dfc09b6a4d6e975edfc65c5c1
https://pubmed.ncbi.nlm.nih.gov/10092863

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