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A disulfide crosslink between Cys98 of troponin-C and Cys133 of troponin-I abolishes the activity of rabbit skeletal troponin.

Various thio-reactive bifunctional crosslinkers as well as 5,5'-dithiobis(2-nitrobenzoate)-mediated disulfide bond formation were used to crosslink troponin-C and troponin-I, the Ca(2+)-binding and inhibitory subunits of troponin, respectively. In all cases, substantial crosslinking was obtaine...

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Main Authors: Park, H S, Gong, B J, Tao, T
Format: Artigo
Jezik:Inglês
Izdano: 1994
Teme:
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC1275931/
https://ncbi.nlm.nih.gov/pubmed/8075339
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