Refolding of bovine threonine-neochymotrypsinogen.

  title={Refolding of bovine threonine-neochymotrypsinogen.},
  author={C. Duda and A. Light},
  journal={The Journal of biological chemistry},
  volume={257 16},
  • C. Duda, A. Light
  • Published 1982
  • Medicine, Chemistry
  • The Journal of biological chemistry
The mixed disulfide derivative of fully reduced neochymotrypsinogen was refolded at pH 9.2 and 4 degrees C with 4 mM cysteine as the disulfide interchange catalyst. The yield of regenerated neochymotrypsinogen was 25%; the corresponding yield of refolded chymotrypsinogen was 50%. The refolded neochymotrypsinogen exhibited the characteristics of the native molecule as determined from polyacrylamide gel electrophoresis and the enzymatic properties of the activated zymogen. The rate of refolding… Expand
Refolding of serine proteinases
The lack of dependence on the concentration of either fragmènt and the relatively high yields suggest independent folding of the amino‐ and carboxyl‐terminal domains. Expand
Detection of intermediate species in the refolding of bovine trypsinogen.
The mixed disulfide of bovine trypsinogen and glutathione was refolded at pH 8.6 and 4 degrees C and produced a partly folded structure with an apparent hydrodynamic volume and the rate of formation of the native structure was determined from the progress curves derived from isoelectric focusing and size-exclusion chromatography. Expand
Behavior of chymotrypsinogen during low pH gel electrophoresis is altered by persulfate.
  • W. G. Moore
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 1986
Chymotrypsinogen was observed to have two bands in a low-pH gel electrophoresis system, though the protein was pure by other criteria, and the affected amino acid residue was identified as tryptophan by titration of persulfate-treated proteins with 2-hydroxy-5-nitrobenzyl bromide and by the spectral method of Edelhoch. Expand
Expression and Folding of Recombinant Bovine Prethrombin-2 and Its Activation to Thrombin (*)
Results indicate that prethrombin-2 was folded into a conformation similar to that of the wild-type protein, and suggest that the carbohydrate on the B chain of wild- type thrombin does not affect the amidolytic and fibrinolytic activities of throm bin. Expand
The Effect of Internal Autocleavage on Kinetic Properties of the Human Cytomegalovirus Protease Catalytic Domain (*)
It is concluded that I site cleavage does not inactivate the HCMV protease, in the absence of other virally induced factors, and that limited potential exists for the regulation of catalytic activity by I site Cleavage. Expand
Covalent hybrids of ovomucoid third domains made from one synthetic and one natural peptide chain.
This work shows that making the covalent hybrids from synthetic and natural material is a facile and efficient method for preparing variants for highly quantitative sequence to reactivity studies, and the first five NH2-terminal residues of avian ovomucoid third domains have no effect on inhibitory activity. Expand
Isolation, renaturation, and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodies
Which methods originally developed for studying the folding mechanism of naturally occurring proteins have been successfully adapted for reactivation of recombinant eukaryotic proteins are shown. Expand
Unfolding Simulations Reveal the Mechanism of Extreme Unfolding Cooperativity in the Kinetically Stable α-Lytic Protease
It is shown that αLP unfolds extremely cooperatively while trypsin unfolds gradually, and a novel method of calculating unfolding cooperativity is proposed, involving three key regions that differ between the kinetically stable and thermodynamically stable classes of serine proteases. Expand
Chemical Basis of Thrombin Interactions with Fibrinogen a
  • H. Scheraga
  • Chemistry, Medicine
  • Annals of the New York Academy of Sciences
  • 1986
Immunoelectron microscopf reveals that the site of thrombin action is in the central nodule of the linear trinodular structure of fibrinogen, and that residues 240-424 of the A a chains5 and the C-terminal portions of the y chains containing the other polymerization sites are in the two outer nodules. Expand


Principles of Protein Structure
1 Amino Acids.- 1.1 The 20 Standard Amino Acids.- 1.2 Why Were Just These Amino Acids Selected?.- 1.3 Colinear Relation Between Nucleic Acids and Polypeptides.- 1.4 Side Chain Properties.- 1.5Expand
Adu. Protein Chern
  • Biochem. Biophys. Res
  • 1975
Methods Enzymol
  • 1967