Results 161 to 170 of about 49,239 (220)

Co-aggregation of annexin A11 and TDP-43 in FTLD/MND with primary lateral sclerosis phenotype. [PDF]

open access: yesActa Neuropathol Commun
Tarutani A   +15 more
europepmc   +1 more source

Double-Stapled Peptide Scan Yields Potent Fusion Inhibitors of Respiratory Syncytial Virus. [PDF]

open access: yesJ Med Chem
Pidoux N   +16 more
europepmc   +1 more source

An Orally Administered Misuse Deterrent Opioid Prodrug for Treatment of Acute Pain. [PDF]

open access: yesJACS Au
Rose DA   +10 more
europepmc   +1 more source
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Allergy to chymotrypsin

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
openaire   +2 more sources

Porcine Chymotrypsin A-π, a More Acidic Chymotrypsin

Canadian Journal of Biochemistry, 1975
A 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
openaire   +2 more sources

The hydrogen-ion equilibria of α-chymotrypsin, monoacetyl-α-chymotrypsin and diisopropylphosphoryl-α-chymotrypsin

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
openaire   +2 more sources

Physicochemical investigation of the chymotrypsins. II. On the mechanism of dimerization of chymotrypsin

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
openaire   +2 more sources

Acetaldehyde Inhibits Chymotrypsin and Serum Anti-Chymotrypsin Activity

Journal of Investigative Medicine, 1998
Background 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
openaire   +2 more sources

Stability of Alpha-Chymotrypsin

Archives of Ophthalmology, 1961
Following 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
openaire   +2 more sources

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