Abstract:
:The effect of removal of Ca2+ bound to thrombospondin (TSP) on the protein structure in solution has been investigated using ESR spin-label techniques. A maleimide spin label was selectively attached to the free thiol group presumably near the carboxyl-terminal domain in which Ca2+-binding sites are situated. The ESR spectra of spin-labeled TSP showed that the bound label undergoes a relatively fast rotational motion with an effective rotational correlation time in the nano-second time regimes. Removal of bound Ca2+ in TSP by dialyzing spin-labeled TSP from a Ca2+-containing buffer into an EDTA-containing buffer resulted in an increase in the mobility of the bound label by a factor of 2.3. The data suggest that EDTA chelation of bound Ca2+ in TSP induces a conformational change of TSP at least near the site of spin labeling.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Slane JM,Mosher DF,Lai CSdoi
10.1016/0014-5793(88)81157-8subject
Has Abstractpub_date
1988-03-14 00:00:00pages
363-6issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(88)81157-8journal_volume
229pub_type
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