Results 251 to 260 of about 118,118 (316)
Allosteric activation mechanism of DriD, a WYL-domain containing transcription regulator. [PDF]
Commun BiolCannistraci E +5 more
europepmc +1 more source
Immunoproteasome remodeling in senescing human macrophages reveals the loss of PA28αβ capping as a hallmark of immunosenescence. [PDF]
Commun BiolMonittola F +13 more
europepmc +1 more source
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Journal of Biomolecular Structure and Dynamics, 2020
Recently, the world has witnessed outbreak of a novel Coronavirus (SARS-CoV-2), the virus which initially emerged in Wuhan, China has now made its way to a large part of the world, resulting in a public emergency of international concern.
S. Khan +4 more
semanticscholar +1 more source
Recently, the world has witnessed outbreak of a novel Coronavirus (SARS-CoV-2), the virus which initially emerged in Wuhan, China has now made its way to a large part of the world, resulting in a public emergency of international concern.
S. Khan +4 more
semanticscholar +1 more source
Journal of Allergy, 1957
HIS report presents a case of allergic sensitivity to chymotrypsin (bovine) in a laboratory worker. The sensitivity apparently was induced by inhalation of the powdered material. With the increasing use of purified enzyme preparations, the hazard of sensitization should be recognized.
Walter R. MacLaren +3 more
openaire +3 more sources
HIS report presents a case of allergic sensitivity to chymotrypsin (bovine) in a laboratory worker. The sensitivity apparently was induced by inhalation of the powdered material. With the increasing use of purified enzyme preparations, the hazard of sensitization should be recognized.
Walter R. MacLaren +3 more
openaire +3 more sources
Porcine Chymotrypsin A-π, a More Acidic Chymotrypsin
Canadian Journal of Biochemistry, 1975A kinetic study of porcine chymotrypsin A-π revealed two characteristic properties of this type of chymotrypsin:1. Porcine chymotrypsin A-π, like bovine chymotrypsin B-π, does not bind proflavin. which is a competitive inhibitor of bovine trypsin and chymotrypsin A-α.2.
E de Médicis, Louise Bergeron
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Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
Abstract Based on the titration curves, the hydrogen-ion equilibria of α-chymotrypsin (EC 3.4.4.5), monoacetyl-α-chymotrypsin and diisopropylphosphoryl-α-chymotrypsin are identical within experimental error. This finding rules out various mechanisms which require the masking or the release of an ionizing residue for catalytic activity.
F. Behr, Mario A. Marini
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Abstract Based on the titration curves, the hydrogen-ion equilibria of α-chymotrypsin (EC 3.4.4.5), monoacetyl-α-chymotrypsin and diisopropylphosphoryl-α-chymotrypsin are identical within experimental error. This finding rules out various mechanisms which require the masking or the release of an ionizing residue for catalytic activity.
F. Behr, Mario A. Marini
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A conjugate of trypsin and chymotrypsin
Applied Biochemistry and Biotechnology, 1987A heteroenzyme conjugate retaining activities of two component enzymes from trypsin and chymotrypsin was prepared using N-succinimidyl pyridyl dithiopropionate as crosslinking reagent. The conjugate bound to both trypsin and chymotrypsin affinity columns. Trypsin and chymotrypsin were linked in the ratio of 1:1 on mol basis. The conjugate, when treated
Munishwar N. Gupta, Y. S. Rajput
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Inactivation of kinins by chymotrypsin
Biochemical Pharmacology, 1976Abstract The inactivation rate of synthetic bradykinin (BK) by different samples of crystallized α-chymotrypsin at pH 7.0, 30° and a 1:10 enzyme/substrate molar ratio was reduced in the presence of 1,10-phenanthroline. Selective inaetivation of the samples by preincubation with l -(1-tosylamido-2-phenyl) ethyl-chloromethylketone (TPCK) in 1:10 ...
Sampaio, CAM +4 more
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