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The pigeon tick (Argas reflexus): its biology, ecology, and epidemiological aspects
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Axelrodia riesei, a new characoid fish from Upper Rio Meta in Colombia With remarks concerning the genus Axelrodia and description of a similar, sympatric, Hyphessobrycon-species
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Proteinase proteinase inhibitor complexes nmr evidence for the protonation state of the charge relay in complexes of bovine pancreatic trypsin inhibitor kunitz with porcine trypsin and bovine chymotrypsin


Proteinase proteinase inhibitor complexes nmr evidence for the protonation state of the charge relay in complexes of bovine pancreatic trypsin inhibitor kunitz with porcine trypsin and bovine chymotrypsin



Federation Proceedings 35(7): 545



ISSN/ISBN: 0014-9446


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Accession: 027231688

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Related references

Effects of proteinase--inhibitor binding on accessibility of exposed tyrosines. A photochemically induced dynamic nuclear polarization study of bovine pancreatic trypsin inhibitor complexes with trypsin, chymotrypsin, and their zymogens. Biochemistry 21(16): 3775-3779, 1982

Binding of native and [homoserine lactone-52]-52,53-seco-bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor) to porcine pancreatic beta-kallikrein-B and bovine alpha-chymotrypsin: thermodynamic study. Journal of Molecular Recognition: Jmr 7(1): 39-46, 1994

Kunitz type proteinase inhibitors derived by limited proteolysis of the inter alpha trypsin ec 3.4.21.4 inhibitor 8. characterization of the bovine inhibitor as double headed trypsin elastase inhibitor. Hoppe Seyler's Zeitschrift fuer Physiologische Chemie 364(12): 1689-1696, 1983

Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, VII. Characterization of the bovine inhibitor as double-headed trypsin-elastase inhibitor. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 364(12): 1689-1696, 1983

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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. Journal of Molecular Recognition: Jmr 3(5-6): 192-196, 1990

Kunitz type proteinase inhibitors derived by limited proteolysis of the inter alpha trypsin ec 3.4.21.4 inhibitor 7. determination of the amino acid sequence of the trypsin released inhibitor from bovine inter alpha trypsin inhibitor. Hoppe Seyler's Zeitschrift fuer Physiologische Chemie 364(12): 1679-1688, 1983

Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, VII. Determination of the amino-acid sequence of the trypsin-released inhibitor from bovine inter-alpha-trypsin inhibitor. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 364(12): 1679-1687, 1983

Active site in zymogens. Proton magnetic resonance pH titration curves of histidine-57 in porcine and bovine trypsinogens and in their complexes with bovine pancreatic trypsin inhibitor (Kunitz). Biochemistry 17(22): 4640-4647, 1978

Differences in dissociation of bovine and porcine trypsin from complexes with chicken ovo inhibitor evidence that the 2 binding sites for trypsin on ovo inhibitor are not equivalent. Federation Proceedings 33(5 Part 2): 1375, 1974

Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor beta-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor. Biochemistry 26(11): 3156-3167, 1987

Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor β-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor. Biochemistry (Easton) 26(11): 3156-3162, 1987

Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor b-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor. Biochemistry (American Chemical Society) 26: 56-62, 1987

Hepatocyte uptake of alpha 1-proteinase inhibitor-trypsin complexes in vitro: evidence for a shared uptake mechanism for proteinase complexes of alpha 1-proteinase inhibitor and antithrombin III. Journal of Cellular Biochemistry 25(4): 231-243, 1984