Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0005289,
umls-concept:C0007452,
umls-concept:C0008742,
umls-concept:C0021469,
umls-concept:C0037733,
umls-concept:C0039808,
umls-concept:C0041236,
umls-concept:C0486805,
umls-concept:C0764105,
umls-concept:C1167622,
umls-concept:C1262902,
umls-concept:C1961133,
umls-concept:C2603343,
umls-concept:C2673177
|
| pubmed:issue |
5-6
|
| pubmed:dateCreated |
1991-7-24
|
| pubmed:abstractText |
The effect of pH and temperature on the apparent association equilibrium constant (Ka) for the binding of the soybean Bowman-Birk proteinase inhibitor (BBI) and of its chymotrypsin and trypsin inhibiting fragments (F-C(p), F-T(p) and F-T(t), respectively) to bovine alpha-chymotrypsin (alpha-chymotrypsin) and bovine beta-trypsin (beta-trypsin) has been investigated. On the basis of Ka values, the proteinase inhibitor affinity can be arranged as follows: alpha-chymotrypsin: BBI approximately beta-trypsin:BBI approximately beta-trypsin:F-T(t) approximately beta-trypsin:F-T(p) much greater than alpha-chymotrypsin:F-C(p). F-C(p), F-T(p) and F-T(t) do not inhibit beta-trypsin and alpha-chymotrypsin action, respectively. On lowering the pH from 9.5 to 4.5, values of Ka for BBI, F-C(p), F-T(p) and/or F-T(t) binding to alpha-chymotrypsin and beta-trypsin decrease, thus reflecting the acid-pK shift of the invariant His57 catalytic residue from 7.0, in the free enzymes, to 5.2, in the proteinase:inhibitor complexes. Considering the known molecular models, the observed binding behaviour of BBI, F-C(p), F-T(p) and F-T(t) was related to the inferred stereochemistry of the proteinase:inhibitor contact regions.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0952-3499
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
192-6
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2096886-Animals,
pubmed-meshheading:2096886-Cattle,
pubmed-meshheading:2096886-Chymotrypsin,
pubmed-meshheading:2096886-Hydrogen-Ion Concentration,
pubmed-meshheading:2096886-Peptide Fragments,
pubmed-meshheading:2096886-Protein Binding,
pubmed-meshheading:2096886-Thermodynamics,
pubmed-meshheading:2096886-Trypsin,
pubmed-meshheading:2096886-Trypsin Inhibitor, Bowman-Birk Soybean
|
| pubmed:articleTitle |
Binding of the soybean Bowman-Birk proteinase inhibitor and of its chymotrypsin and trypsin inhibiting fragments to bovine alpha-chymotrypsin and bovine beta-trypsin. A thermodynamic study.
|
| pubmed:affiliation |
Department of Biochemical Sciences, University of Rome La Sapienza, Italy.
|
| pubmed:publicationType |
Journal Article
|