In:
Advanced Synthesis & Catalysis, Wiley, Vol. 345, No. 6-7 ( 2003-06), p. 729-734
Abstract:
β(1→4) Galactosyltransferase expressed as a fusion protein with maltose binding protein (MBP‐GalT) was displayed specifically on a Langmuir–Blodgett (LB) membrane prepared by photopolymerization of maltotriose‐carrying glycolipid ( 1 ) with 1,2‐bis(10,12‐tricosadiynoyl)‐ sn ‐glycero‐3‐phosphocholine ( 2 ). The catalytic activity of MBP‐GalT on the LB film was directly monitored by the surface plasmon resonance (SPR) method using a GlcNAc‐carrying water‐soluble polymer ( 3 ) as an acceptor substrate. Highly sensitive sigmoidal‐type signals were obtained upon the addition of the acceptor substrate in the presence of the donor substrate, UDP‐galactose (UDP‐Gal), while the binding of 3 was not detected in the absence of UDP‐Gal. The intensities of the signals were dependent on the amount of immobilized MBP‐GalT on the LB film, which was estimated from the images obtained by atomic force microscope (AFM).
Type of Medium:
Online Resource
ISSN:
1615-4150
,
1615-4169
DOI:
10.1002/adsc.v345:6/7
DOI:
10.1002/adsc.200202204
Language:
English
Publisher:
Wiley
Publication Date:
2003
detail.hit.zdb_id:
2041384-1
detail.hit.zdb_id:
2033084-4
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