Title : Characterization of zero-length cross-links between rabbit skeletal muscle troponin C and troponin I: evidence for direct interaction between the inhibitory region of troponin I and the NH2-terminal, regulatory domain of troponin C.

Pub. Date : 1990 Jan 9

PMID : 2108719






5 Functional Relationships(s)
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1 In an attempt to identify other possible physiologically important interactions between these proteins, 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC) was used to produce zero-length cross-links in the complex of rabbit skeletal muscle TnC and TnI. Ethyldimethylaminopropyl Carbodiimide tenascin Oryctolagus cuniculus
2 In an attempt to identify other possible physiologically important interactions between these proteins, 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC) was used to produce zero-length cross-links in the complex of rabbit skeletal muscle TnC and TnI. Ethyldimethylaminopropyl Carbodiimide tenascin Oryctolagus cuniculus
3 TnC was activated with EDC and N-hydroxysuccinimide (NHS) and then mixed with an equimolar amount of TnI [Grabarek, Z., & Gergely, J. Ethyldimethylaminopropyl Carbodiimide tenascin Oryctolagus cuniculus
4 TnC was activated with EDC and N-hydroxysuccinimide (NHS) and then mixed with an equimolar amount of TnI [Grabarek, Z., & Gergely, J. N-hydroxysuccinimide tenascin Oryctolagus cuniculus
5 TnC was activated with EDC and N-hydroxysuccinimide (NHS) and then mixed with an equimolar amount of TnI [Grabarek, Z., & Gergely, J. N-hydroxysuccinimide tenascin Oryctolagus cuniculus