Results 191 to 200 of about 57,869 (249)
An Orally Administered Misuse Deterrent Opioid Prodrug for Treatment of Acute Pain. [PDF]
JACS AuRose DA +10 more
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A quest for greater thermodynamic rigour in the quantitative characterization of protein self-association by direct assessment of sedimentation equilibrium distributions. [PDF]
Biophys RevWinzor DJ, Wills PR.
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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.
F, ALADJEM, W R, MACLAREN
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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.
F, ALADJEM, W R, MACLAREN
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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, L, 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.
M A, MARINI, F, BEHR
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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.
M A, MARINI, F, BEHR
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Archives of Biochemistry and Biophysics, 1957
Summary 1. The sedimentation velocity of α -chymotrypsin was studied as a function of protein concentration and pH. The complete loss of dimerizability for α -chymotrypsin between pH 3.6 and 2.3 points to the involvement of a carboxylate ion—probably contributed by aspartic acid—in the formation of the double molecule of α -chymotrypsin.
R, EGAN +3 more
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Summary 1. The sedimentation velocity of α -chymotrypsin was studied as a function of protein concentration and pH. The complete loss of dimerizability for α -chymotrypsin between pH 3.6 and 2.3 points to the involvement of a carboxylate ion—probably contributed by aspartic acid—in the formation of the double molecule of α -chymotrypsin.
R, EGAN +3 more
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Acetaldehyde Inhibits Chymotrypsin and Serum Anti-Chymotrypsin Activity
Journal of Investigative Medicine, 1998Background Chymotrypsin (CT) and CT-like enzymes contribute to the dynamics of metabolism by their participation in digestion, peptide hormone generation and catabolism, fertilization of ova and inhibition of thrombin-induced platelet aggregation, among other processes.
A S, Brecher, M P, Yang
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Stability of Alpha-Chymotrypsin
Archives of Ophthalmology, 1961Following the early reports by Barraquer 1 and Jenkins 2 on the use of α-chymotrypsin in cataract surgery, ophthalmic surgeons have shown considerable interest in the further development of this new technique. This communication details results that indicate by both biochemical assay and clinical experience, at least one commercial α-chymotrypsin ...
L F, WATTS, C J, MARTIN
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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
Y S, Rajput, M N, Gupta
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Biochemistry, 1994
We have examined the reaction of N-(benzyloxycarbonyl)-L-alanyl-L-glycyl-L-phenylalanyl chloromethyl ketone (ZAGFCMK) with chymotrypsin (Cht) and have found that, in addition to irreversible alkylation of the enzyme, some of the corresponding hydroxymethyl ketone is produced. For each molecule of hydroxy ketone formed, 3.6 molecules of chymotrypsin are
M, Prorok +3 more
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We have examined the reaction of N-(benzyloxycarbonyl)-L-alanyl-L-glycyl-L-phenylalanyl chloromethyl ketone (ZAGFCMK) with chymotrypsin (Cht) and have found that, in addition to irreversible alkylation of the enzyme, some of the corresponding hydroxymethyl ketone is produced. For each molecule of hydroxy ketone formed, 3.6 molecules of chymotrypsin are
M, Prorok +3 more
openaire +2 more sources