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Journal ArticleDOI

Further observations on substrate-derived chloromethyl ketones that inactivate trypsin.

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TLDR
In this article, the inactivation of trypsin by TLCK was examined with respect to dependence on the concentration of the inhibitor and Saturation kinetics were observed as expected of an active-site directed reagent.
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This article is published in Archives of Biochemistry and Biophysics.The article was published on 1970-08-01. It has received 67 citations till now. The article focuses on the topics: Trypsin.

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Citations
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Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin-like snake venom enzyme.

TL;DR: The nucleotide sequence of a cDNA for batroxobin, a thrombin-like enzyme from Bothrops atrox, moojeni venom, allowed elucidation of the complete amino acid sequence of Batroxobin for the first time, indicating that batroxobar is a member of the serine protease family.
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The Purification of Thrombin and Isolation of a Peptide Containing the Active Center Histidine

TL;DR: A radioactive peptide has been isolated from thrombin inactivated with tritiated Nα-tosyl lysyl chloromethyl ketone and shown to contain histidine-43, showing loss of both clotting and esterase activities.
Journal ArticleDOI

Protease II from Escherichia coli. Purification and characterization.

TL;DR: Differences in protease susceptibility can be related to the conformational state of the substrate, and the possible implication of structural changes in the mechanism of preferential proteolysis in vivo is discussed.
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Identification of a Reactive Cysteine Residue at the Glutamine Binding Site of Carbamyl Phosphate Synthetase

TL;DR: Investigation of Carbamyl phosphate synthetase from Escherichia coli indicates that the chloroketone reacts with a sulfhydryl group at the glutamine site of the light subunit, suggesting that it is buried.
References
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The preparation and properties of two new chromogenic substrates of trypsin.

TL;DR: Preliminary studies indicate that benzoyl dl -arginine p -nitroanilide hydrochloride is also hydrolyzed by papain, and that of l -LPA is in a more alkaline region than normally found for trypsin substrates.
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A spectrophotometric determination of trypsin and chymotrypsin

TL;DR: A sensitive spectrophotometric assay for trypsin and chymotrypsin using synthetic substrates has been described.
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