High impact information on LOC529639

• Chymotrypsinogen C displays structural features characteristic for chymotrypsins as well as elastases, except for its activation domain; similar to bovine chymotrypsinogen A, its binding site is not properly formed, while its surface located activation segment is disordered [1].
• Ionic interactions between bovine chymotrypsinogen A and chondroitin sulfate A.B.C.. A possible model for molecular aggregation in zymogen granules [2].
• The seven first residues of subunit III are identical to residues 18-24 of bovine chymotrypsinogen B and very similar with the same residues in bovine chymotrypsinogen A and C (subunit II) and also in proelastase A of the African lungfish [3].
• Seven secretory proteins (chymotrypsinogen A, trypsinogen, carboxypeptidase A, RNase, DNase, alpha-amylase and lipase) were localized in normal bovine pancreatic acinar cells but in diabetic animals amylase, lipase and carboxypeptidase were either not detectable or markedly diminished [4].
• Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type) [5].

Biological context of LOC529639

• Temperature-dependence of the kinetics of folding of chymotrypsinogen A [6].
• Ribonuclease A was thermally unstabilized by reductive alkylation, while chymotrypsinogen A was slightly stabilized, depending on both the size of the introduced alkyl groups and the extent of modification [7].

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

• As models of this domain, bovine beta-trypsin, trypsinogen, alpha-chymotrypsin and chymotrypsinogen A were studied by neutron and X-ray synchrotron solution scattering [13].

Analytical, diagnostic and therapeutic context of LOC529639

• Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin Aalpha [12].
• The thermal denaturation of chymotrypsinogen A was investigated by differential scanning calorimetry in the water-content range 0.09 -1.46 g water per g protein [14].

References