Abstract:
:A truncated human Na(+)/glucose cotransporter (C(5), residues 407-664) was expressed and purified from Escherichia coli using a GST fusion vector and glutathione affinity chromatography. The truncated transporter (C(5)) was cleaved from GST-C(5) by Factor Xa proteolysis and purified by gel filtration chromatography. Up to 1 mg of purified GST-C(5) was obtained from 1 l bacterial culture. Reconstitution of both GST-C(5) and C(5) proteins into lipid vesicles resulted in 2.5-fold higher initial uptake rates of [(3)H]D-glucose into C(5)-proteoliposomes than into liposomes. Transport was stereospecific, saturable, and inhibited by phloretin. These properties are similar to those obtained for C(5) in Xenopus laevis oocytes, and provide additional evidence that the five C-terminal transmembrane helices in SGLT1 form the sugar translocation pathway.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Panayotova-Heiermann M,Leung DW,Hirayama BA,Wright EMdoi
10.1016/s0014-5793(99)01292-2keywords:
subject
Has Abstractpub_date
1999-10-15 00:00:00pages
386-90issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01292-2journal_volume
459pub_type
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