The recombinant fucolectin-related protein (FRP) of unknown function, encoded by the SP2159 gene of was expressed in . In this study, its glycan-recognition epitopes and their binding potencies were examined by enzyme-linked lectinosorbent and inhibition assays. The results indicate that FRP reacted strongly with human blood group and l-Fucα1→2-active glycotopes and in their polyvalent (super) forms. When expressed by mass relative potency, the binding affinities of FRP to poly-l-Fucα1→glycotopes were about 5.0 × 10 folds higher than that of the mono-l-Fucα1→glycotope form. This unique binding property of FRP can be used as a special tool to differentiate complex forms of l-Fucα1→2 and other forms of glycotopes.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5991896 | PMC |
http://dx.doi.org/10.1016/j.biopen.2017.12.002 | DOI Listing |
Biochim Open
June 2018
Department of Biochemistry and Molecular Biology, Tulane University, School of Medicine, 1430 Tulane Ave., New Orleans, LA 70112, USA.
The recombinant fucolectin-related protein (FRP) of unknown function, encoded by the SP2159 gene of was expressed in . In this study, its glycan-recognition epitopes and their binding potencies were examined by enzyme-linked lectinosorbent and inhibition assays. The results indicate that FRP reacted strongly with human blood group and l-Fucα1→2-active glycotopes and in their polyvalent (super) forms.
View Article and Find Full Text PDFWe previously purified Streptococcus mitis-derived human platelet aggregation factor (Sm-hPAF) from the culture supernatant of S. mitis strain Nm-65, isolated from the tooth surface of a patient with Kawasaki disease. Here we produced recombinant Sm-hPAF protein (rSm-hPAF) in Escherichia coli, to determine whether rSm-hPAF conserves its platelet aggregation activity.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!