Xylosyltransferase I acceptor properties of fibroblast growth factor and its fragment bFGF (1-24).

摘要: Abstract Human basic fibroblast growth factor (bFGF) is a heparin-binding containing G-S-G-motif which potential recognition sequence of xylosyltransferase I (XT-I). Here, we show that the recombinant human bFGF was xylosylated in vitro by XT-I and fragment (1–24) good acceptor ( K m  = 20.8 μM for native  = 22.3 μM XT-I). MALDI MALDI-PSD time-of-flight mass spectrometric analyses protein demonstrate transfer xylose to serine residue amino terminal end bFGF. The peptide well suitable as an substrate can be used radiochemical assay measure activity cell culture supernatant body fluids, respectively. Furthermore, could interacts strongly with heparin this glycosaminoglycan predominantly non-competitive inhibitor enzyme using acceptor.