Abstract:
:Association reactions of a recombinant CFTR-NBF-2 polypeptide fused to glutathione S-transferase with guanine nucleotides were monitored quantitatively by recording the fluorescence enhancement of excited trinitrophenol (TNP)-labelled GTP after binding to NBF-2. Binding of TNP-GTP to the recombinant NBF-2 polypeptide was characterized by a Kd value of 3.9 microM. The corrected Kd values for unlabelled guanine nucleotides were determined to be 33 microM for GTP, 92 microM for GDP and 217 microM for GMP. TNP-ATP bound to NBF-2 was competitively displaced by GTP indicating a common binding site for both nucleotides. The recombinant NBF-2 did not show an intrinsic GTPase activity above a detection limit of 0.007 min(-1). Our findings provide the first experimental evidence that NBF-2 can act as a GTP-binding subunit that would favor the release of GDP after GTP hydrolysis.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Randak C,Neth P,Auerswald EA,Assfalg-Machleidt I,Roscher AA,Hadorn HB,Machleidt Wdoi
10.1016/s0014-5793(96)01217-3subject
Has Abstractpub_date
1996-11-25 00:00:00pages
97-100issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(96)01217-3journal_volume
398pub_type
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