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CTRB2  -  chymotrypsinogen B2

Bos taurus

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High impact information on LOC529639


Biological context of LOC529639


Anatomical context of LOC529639

  • When porcine alpha-amylase or bovine chymotrypsinogen A was added to the medium bathing the rabbit pancreas in short-term organ culture, the secretion of these enzymes collected via the duct system increased greatly [8].

Associations of LOC529639 with chemical compounds

  • In this paper, this hypothesis was tested by studies on the interactions between bovine chymotrypsinogen A and chondroitin sulfate as a simplified model [2].
  • The X-ray structure of a new crystal form of chymotrypsinogen A grown from ethanol/water has been determined at 1.8 A resolution using Patterson search techniques [9].
  • Protonation-state dependence of hydrogen bond strengths and exchange rates in a serine protease catalytic triad: bovine chymotrypsinogen A [10].
  • These include the NH2-terminal four residues, the sequences near histidine-57 (chymotrypsinogen A numbering system), aspartic acid-102, aspartic acid-189, and serine-195, the regions of the three disulfide bridges, and the COOH-terminal end (residues 225-229) of the proteins [11].
  • Reversible unfolding of bovine chymotrypsinogen A in 2H2O either by heating at low pH or by exposure to 6 M guanidinium chloride results in the exchange of virtually all the nitrogen-bound hydrogens that give rise to low-field 1H NMR peaks, without significant exchange of the histidyl ring Cepsilon1 hydrogens [12].

Other interactions of LOC529639


Analytical, diagnostic and therapeutic context of LOC529639


  1. The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C. Gomis-Rüth, F.X., Gómez, M., Bode, W., Huber, R., Avilés, F.X. EMBO J. (1995) [Pubmed]
  2. Ionic interactions between bovine chymotrypsinogen A and chondroitin sulfate A.B.C.. A possible model for molecular aggregation in zymogen granules. Reggio, H., Dagorn, J.C. J. Cell Biol. (1978) [Pubmed]
  3. Dissociation of bovine 6S procarboxypeptidase A by reversible condensation with 2,3-dimethyl maleic anhydride: application to the partial characterization of subunit III. Puigserver, A., Desnuelle, P. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  4. Alterations of exocrine pancreatic enzymes in virus-induced diabetic cattle as revealed by immunohistochemistry. Bendayan, M., Ito, S., Manocchio, I. Diabetologia (1982) [Pubmed]
  5. Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type). Hecht, H.J., Szardenings, M., Collins, J., Schomburg, D. J. Mol. Biol. (1991) [Pubmed]
  6. Temperature-dependence of the kinetics of folding of chymotrypsinogen A. Pohl, F.M. FEBS Lett. (1976) [Pubmed]
  7. Effect of reductive alkylation on thermal stability of ribonuclease A and chymotrypsinogen A. Fujita, Y., Noda, Y. Int. J. Pept. Protein Res. (1991) [Pubmed]
  8. Transpancreatic transport of digestive enzyme. Isenman, L.D., Rothman, S.S. Biochim. Biophys. Acta (1979) [Pubmed]
  9. Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution. Wang, D., Bode, W., Huber, R. J. Mol. Biol. (1985) [Pubmed]
  10. Protonation-state dependence of hydrogen bond strengths and exchange rates in a serine protease catalytic triad: bovine chymotrypsinogen A. Markley, J.L., Westler, W.M. Biochemistry (1996) [Pubmed]
  11. Amino acid sequence of Streptomyces griseus trypsin. Cyanogen bromide fragments and complete sequence. Olafson, R.W., Jurásek, L., Carpenter, M.R., Smillie, L.B. Biochemistry (1975) [Pubmed]
  12. Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin Aalpha. Markley, J.L., Ibañez, I.B. Biochemistry (1978) [Pubmed]
  13. Modelling of the serine-proteinase fold by X-ray and neutron scattering and sedimentation analyses: occurrence of the fold in factor D of the complement system. Perkins, S.J., Smith, K.F., Kilpatrick, J.M., Volanakis, J.E., Sim, R.B. Biochem. J. (1993) [Pubmed]
  14. Effect of hydration on the thermal stability of protein as measured by differential scanning calorimetry. Chymotrypsinogen A. Fujita, Y., Noda, Y. Int. J. Pept. Protein Res. (1981) [Pubmed]
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