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Incomplete refolding of a fragment of the N-terminal domain of pig muscle 3-phosphoglycerate kinase that lacks a subdomain. Comparison with refolding of the complementary C-terminal fragment.
Szilágyi AN, Kotova NV, Semisotnov GV, Vas M. Szilágyi AN, et al. Among authors: vas m. Eur J Biochem. 2001 Mar;268(6):1851-60. Eur J Biochem. 2001. PMID: 11248706 Free article.
Refolding of pig muscle 3-phosphoglycerate kinase (PGK) from a mixture of its complementary proteolytic fragments that did not correspond to the individual domains resulted in a high degree of reactivation [Vas, M., Sinev, M.A., Kotova, N. & Semisotnov, G …
Refolding of pig muscle 3-phosphoglycerate kinase (PGK) from a mixture of its complementary proteolytic fragments that did not correspond to …
Reactivation of 3-phosphoglycerate kinase from its unfolded proteolytic fragments.
Vas M, Sinev MA, Kotova NV, Semisotnov GV. Vas M, et al. Eur J Biochem. 1990 May 20;189(3):575-9. doi: 10.1111/j.1432-1033.1990.tb15525.x. Eur J Biochem. 1990. PMID: 2351137 Free article.
Limited trypsinolysis of pig muscle 3-phosphoglycerate kinase yielded a nicked enzyme without loss of catalytic activity [Jiang, S. X. & Vas, M. (1988) FEBS Lett. 231, 151-154]. The reactivation rate of the nicked enzyme after denaturation does not differ substa …
Limited trypsinolysis of pig muscle 3-phosphoglycerate kinase yielded a nicked enzyme without loss of catalytic activity [Jiang, S. X. & …
138 results