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Page 1
Independent refolding of domains in the pancreatic serine proteinases.
Higaki JN, Light A. Higaki JN, et al. Among authors: light a. J Biol Chem. 1986 Aug 15;261(23):10606-9. J Biol Chem. 1986. PMID: 3525551 Free article.
The mixed disulfide derivative of Ser-neotrypsinogen was successfully refolded. A functional molecule was regenerated from the polypeptide fragments with the correct molecular weight of neotrypsinogen in an overall yield of 7%. ...The same kinetic results were also found i …
The mixed disulfide derivative of Ser-neotrypsinogen was successfully refolded. A functional molecule was regenerated from the polype …
Further evidence for independent folding of domains in serine proteases.
Light A, al-Obeidi AM. Light A, et al. J Biol Chem. 1991 Apr 25;266(12):7694-8. J Biol Chem. 1991. PMID: 2019593 Free article.
The folding pathway of pancreatic serine proteases was clarified from kinetic studies on the refolding of the glutathione-mixed disulfide derivative of bovine neochymotrypsinogen. Neochymotrypsinogen is prepared from a limited proteolysis of native chymotrypsinogen A …
The folding pathway of pancreatic serine proteases was clarified from kinetic studies on the refolding of the glutathione-mixed disulfide de …
Refolding of serine proteinases.
Light A, Duda CT, Odorzynski TW, Moore WG. Light A, et al. J Cell Biochem. 1986;31(1):19-26. doi: 10.1002/jcb.240310104. J Cell Biochem. 1986. PMID: 3522609
We then refolded threonine-neochymotrypsinogen, which is a two-chain structure held together by disulfide bonds and produced on cleavage of Tyr 146-Thr 147 in native chymotrypsinogen [Duda CT, Light A, J Biol Chem 257 9866-9871, 1982]. ...
We then refolded threonine-neochymotrypsinogen, which is a two-chain structure held together by disulfide bonds and produced on cleav …
Size-exclusion high performance liquid chromatography of native trypsinogen, the denatured protein, and partially refolded molecules. Further evidence that non-native disulfide bonds are dominant in refolding the completely reduced protein.
al-Obeidi AM, Light A. al-Obeidi AM, et al. Among authors: light a. J Biol Chem. 1988 Jun 25;263(18):8642-5. J Biol Chem. 1988. PMID: 3379038 Free article.
Rechromatography of a series of fractions collected at a specific urea concentration showed that each had the same Stokes radius as the fraction in the initial separation. ...These observations support the suggestion that non-native disulfide bonds are responsible f …
Rechromatography of a series of fractions collected at a specific urea concentration showed that each had the same Stokes radi …
The preparation and properties of the catalytic subunit of bovine enterokinase.
Light A, Fonseca P. Light A, et al. J Biol Chem. 1984 Nov 10;259(21):13195-8. J Biol Chem. 1984. PMID: 6386810 Free article.
The conditions separated the heavy and light subunits quantitatively with improved reliability when compared to the conditions used previously (Savithri, H. S., and Light, A. (1980) Biochim. Biophys. Res. Commun, 94, 360-365). Pancreatic trypsin inhibitor was …
The conditions separated the heavy and light subunits quantitatively with improved reliability when compared to the conditions used p …
381 results