Limited proteolysis and chemical cross-linking techniques have been used to study the interaction between α- and β-tubulin subunits. Trypsin digestion of tubulin dimer resulted in the cleavage of the α-subunit into two fragments, whereas chymotrypsin cleaved the β-subunit into two distinct fragments. All of these fragments have been mapped on the tubulin subunits by further proteolysis with formic acid. Cross-linking of trypsin- and chymotrypsin-cleaved subunits has been performed with two different cross-linker agents of different cross-linking distance. The addition of formaldehyde resulted in the cross-linking of the α-tubulin N-terminal fragment with β-tubulin C-terminal domain. The same result was obtained when methyl 4-mercaptobutyrimidate was used.
Research Article|September 01 1985
The interaction between subunits in the tubulin dimer
Biochem J (1985) 230 (2): 551-556.
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L Serrano, J Avila; The interaction between subunits in the tubulin dimer. Biochem J 1 September 1985; 230 (2): 551–556. doi: https://doi.org/10.1042/bj2300551
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