In:
European Journal of Biochemistry, Wiley, Vol. 160, No. 1 ( 1986-10), p. 83-91
Kurzfassung:
Maltooligosaccharides with two to six (α1–4)‐linked glucose residues, carrying at their reducing end a 3‐azi‐1‐methoxybutyl group in either α or in β glycosidic linkage, were synthesized. These maltooligosaccharide analogues inhibit maltose uptake via the maltose‐binding‐protein‐dependent transport system in Escherichia coli . The concentration of half‐maximal inhibition of maltose transport, at 15 nM concentration, decreases with increasing chain length of the analogue, levelling off at 40 μM after a chain length of four glucose residues in the α series and at 350 μM after a chain length of three glucose residues in the β series. The inhibition of maltose transport occurs at the level of the periplasmic maltose‐binding protein. 3‐Azi‐1‐methoxybutyl α‐ D ‐[ 3 H]maltotrioside was bound by the maltose‐binding protein with a K d of 0.18 mM. Irradiation at 350 nm of purified maltose‐binding protein in the presence of 4 μM of this substrate labeled the protein covalently; labeling was prevented by 1 mM maltose. Using a crude preparation of periplasmic proteins two proteins were labeled, the maltose‐binding protein and α‐amylase. Thus, 3‐azi‐1‐methoxybutyl α‐ D ‐maltooligosaccharides are potent photoaffinity labels for proteins with maltooligosaccharides‐binding sites.
Materialart:
Online-Ressource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1986.160.issue-1
DOI:
10.1111/j.1432-1033.1986.tb09943.x
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
1986
ZDB Id:
1398347-7
ZDB Id:
2172518-4
SSG:
12
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