One-step biotinylation procedure for carbohydrates to study carbohydrate-protein interactions.
AuthorsGrün CH, van Vliet SJ, Schiphorst WE, Bank CM, Meyer S, van Die I, van Kooyk Y
JournalAnal Biochem
PubMed ID16713984
'Protein-carbohydrate interactions play crucial roles in numerous biological processes. To study these interactions, we developed a simple and fast procedure for the biotinylation of carbohydrates based on reductive amination. The method allows complete and stable biotinylation of small quantities of oligosaccharides and includes a rapid and simple procedure to remove ... More
Detection of protein carbonyls by means of biotin hydrazide-streptavidin affinity methods.
AuthorsHensley K,
JournalMethods Mol Biol
PubMed ID19378083
'Oxidative posttranslational protein modifications occur as a normal process of cell biology and to a greater extent during pathogenic conditions. The detection and quantitation of protein oxidation has posed a continuing challenge to bioanalytical chemists because the products of oxidative protein damage are chemically diverse, protein oxidation generally occurs at ... More
Protein-heparin interactions measured by BIAcore 2000 are affected by the method of heparin immobilization.
AuthorsOsmond RI, Kett WC, Skett SE, Coombe DR
JournalAnal Biochem
PubMed ID12423639
'Surface plasmon resonance (SPR) biosensors such as the BIAcore 2000 are a useful tool for the analysis of protein-heparin interactions. Generally, biotinylated heparin is captured on a streptavidin-coated surface to create heparinized surfaces for subsequent binding analyses. In this study we investigated three commonly used techniques for the biotinylation of ... More
Coupling of monoclonal antibodies with biotin.
AuthorsHaugland RP, You WW
JournalMethods Mol Biol
PubMed ID7550685
Coupling of antibodies with biotin.
AuthorsHaugland RP, You WW
JournalMethods Mol Biol
PubMed ID9664374
Addition of the keto functional group to the genetic code of Escherichia coli.
AuthorsWang L, Zhang Z, Brock A, Schultz PG
JournalProc Natl Acad Sci U S A
PubMed ID12518054
Although the keto group is the most versatile of the functional groups in organic chemistry, it is absent in the genetically encoded amino acids. To overcome this natural limitation on protein biosynthesis, we have evolved an orthogonal tRNA-synthetase pair that makes possible the efficient incorporation of a keto amino acid, ... More
Biotinylation reagents for the study of cell surface proteins.
AuthorsElia G,
JournalProteomics
PubMed ID18763706
The extraordinarily stable, non-covalent interaction between avidin and biotin is one of the most commonly exploited tools in chemistry and biology. Methods for derivatization with biotin of a variety of molecules (in particular, proteins) have been introduced, in order to allow their efficient recovery, immobilization and detection with avidin-based reagents. ... More
A binding site for heparin in the apple 3 domain of factor XI.
AuthorsHo DH, Badellino K, Baglia FA, Walsh PN
JournalJ Biol Chem
PubMed ID9632702
Since heparin potentiates activated factor XI (FXIa) inhibition by protease nexin-2 by providing a template to which both proteins bind (Zhang, Y., Scandura, J. M., Van Nostrand, W. E., and Walsh, P. N. (1997) J. Biol. Chem. 272, 26139-26144), we examined binding of factor XI (FXI) and FXIa to heparin. ... More