Results 191 to 200 of about 87,578 (233)
Integrated metabolome and microbiome analysis deciphers the effects of resveratrol and β-hydroxy-β-methylbutyric acid on jejunal function under different protein levels in Tibetan sheep. [PDF]
Zhu K +10 more
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Dual Regulation of Corneodesmosome Formation by Shotokuseki Extract Enhances Skin Barrier Homeostasis. [PDF]
Tsukui K +4 more
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Comparative shotgun proteomics analysis of wheat gluten proteins digested by various peptidases. [PDF]
Kaemper C +5 more
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Deep-Sea Genome Mining Reveals Cooperative ATP-Grasp Ligase-Directed Biosynthesis of Pentacyclic Myxomiditides with Potent Protease Inhibition. [PDF]
Li Y +5 more
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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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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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Peptide aldehydes inhibiting chymotrypsin
Biochemical and Biophysical Research Communications, 1972Abstract Peptide aldehydes, in which the argininal moiety of leupeptin Ac (Ac-Leu-Leu-argininal) was replaced by phenylalaninal, tyrosinal or tryptophanal, were synthesized. These compounds exhibited potent inhibition on the proteolytic activity of chymotrypsin in contrast with leupeptin which was reported to inhibit trypsin.
A, Ito, K, Tokawa, B, Shimizu
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