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A Smart Bioconjugate of Chymotrypsin [PDF]
Biomacromolecules, 2003 alpha-Chymotrypsin was immobilized on Eudragit S-100 via covalent coupling with 93% retention of proteolytic activity. The conjugate behaved as a smart biocatalyst and functioned as a pH-dependent reversibly soluble-insoluble biocatalyst. The pH optimum of chymotrypsin broadened on immobilization, and the immobilized preparation showed better stability
Moganty R. Rajeswari +4 more
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THE CHEMICAL MODIFICATION OF CHYMOTRYPSIN
Canadian Journal of Biochemistry, 1964Chemical modification of chymotrypsin has led to the identification of several amino acid side-chains which are probably constituents of the active site of the enzyme. A single seryl and a single histidyl residue appear to cooperate in catalyzing the bond-breaking process while one or more tryptophanyl residues may be involved in the specific binding ...
G. H. Dixon, H. Schachter
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The structure of an insect chymotrypsin
Journal of Molecular Biology, 2000The South American imported fire ant (Solenopsis invicta), without natural enemies in the United States, widely infests the southern United States, causing more than a half billion dollars in health and agriculture-related damage annually in Texas alone.
David H. Russell +6 more
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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.
Richard 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.
Richard Egan +3 more
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Coaggregate of trypsin and chymotrypsin [PDF]
Biotechnology and Bioengineering, 1988 AbstractThe method of chemical aggregation of enzymes has the advantage of yielding an immobilized enzyme preparation wherein reactor volume can be significantly reduced because of the absence of an inert carrier. A coaggregate of trypsin and chymotrypsin formed by extensive cross‐linking with glutaraldehyde is described. A significant property of this
Yudhishthir S. Rajput +1 more
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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 ...
Charles J. Martin, Leland F. Watts
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1974
Publisher Summary Chymotrypsins are the products of the tryptic activation of the inactive precursors, the chymotrypsinogens produced by the pancreas of many species. The isolation of bovine chymotrypsinogen and its activation by trypsin were reported some forty years ago.
G. Tomlinson, M.C. Shaw, T. Viswanatha
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Publisher Summary Chymotrypsins are the products of the tryptic activation of the inactive precursors, the chymotrypsinogens produced by the pancreas of many species. The isolation of bovine chymotrypsinogen and its activation by trypsin were reported some forty years ago.
G. Tomlinson, M.C. Shaw, T. Viswanatha
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ANAPHYLACTIC REACTION TO CHYMOTRYPSIN
Journal of the American Medical Association, 1960Proteolytic enzyme therapy has been employed in various diseases in which its anti-inflammatory and fibrinolytic effects have been of value. Among such agents, aqueous chymotrypsin (Chymar) has been described as relatively free of undesirable side-effects.
Daniel Liebowitz, Henry Ritter
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Archives of Ophthalmology, 1966
To the Editor: I read with considerable interest Dr. Michael Hogan's remarks concerning possible deleterious effects of α-chymotrypsin. It might have been more to the point had Dr. Hogan edited the commercial query to read, "Alpha si ? o Alpha no ?". However, since Dr.
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To the Editor: I read with considerable interest Dr. Michael Hogan's remarks concerning possible deleterious effects of α-chymotrypsin. It might have been more to the point had Dr. Hogan edited the commercial query to read, "Alpha si ? o Alpha no ?". However, since Dr.
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Inactivation and Reactivation of Chymotrypsin
Nature, 1961IN previous work on the immediate effects of acylation of trypsin it was shown1 that the enzyme can be obtained in a fully inactive form by acylation with various anhydrides at pH 8–9, and that partial instantaneous reactivation can be effected by treatment with alkaline hydroxylamine2.
T. Therattil Antony, T. Therattil Antony
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