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Stability of Alpha-Chymotrypsin

Authors: Charles J. Martin; Leland F. Watts;

Stability of Alpha-Chymotrypsin

Abstract

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 preparation * can be used repeatedly after solubilization as a chemical adjunct to cataract surgery. Experimental Results The enzyme preparation was solubilized with its accompanying diluent as per manufacturer's directions to give a 1:5,000 dilution (stock enzyme solution). All aliquot removals were performed aseptically. In these experiments 2 separate samples of α-chymotrypsin were used; one for stability studies at 25 C and the other for comparable purposes at 2 C. Residual enzymatic activity was determined at pH 8.0 and 30 C with either N -carbobenzoxy-l-tyrosine p -nitrophenyl ester (CTN) or N -acetyl-ltyrosine ethyl ester (ATEE) as substrates.

Keywords

Chymotrypsin

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
5
Average
Average
Average
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