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Thiirancarboxamides as Inhibitors of Papain
Archiv der Pharmazie, 2004AbstractDerivatives of the thiirancarboxylic acid building‐block containing a peptide bond were synthesised and screened against the model cysteine protease papain. The most active of the series showed a second‐order rate constant of inactivation comparable to that of the parent compound.
Gemma, Bruno, Tanja, Schirmeister
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1971
Publisher Summary The fruits of the tropical papaya tree have latex that contains several enzymes. This chapter focuses on two different proteolytic enzymes: chymopapain and papain. Both enzymes belong to the group of proteolytic plant enzymes that require a sulfhydryl group for activity.
J, Drenth +3 more
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Publisher Summary The fruits of the tropical papaya tree have latex that contains several enzymes. This chapter focuses on two different proteolytic enzymes: chymopapain and papain. Both enzymes belong to the group of proteolytic plant enzymes that require a sulfhydryl group for activity.
J, Drenth +3 more
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Biochemical and Biophysical Research Communications, 1970
Abstract Papain possesses several regions of internal homology and similar shape. The enzyme probably formed through a series of gene doublings.
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Abstract Papain possesses several regions of internal homology and similar shape. The enzyme probably formed through a series of gene doublings.
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Modification of Papain with Tetranitromethane
The Journal of Biochemistry, 1978Papain [EC 3.4.22.2] polymerizes readily upon treatment with tetranitromethane (TNM) by forming intermolecular covalent linkages through its tyrosine residues (Tsukamoto, S. & Ohno, M. (1974) J. Biochem. 75, 1377-1380). Polymerization occurred optimally at pH 9.0 with S-sulfenylsulfonate papain. Circular dichroic spectra of polymerized papains showed a
S, Tsukamoto, M, Ohno
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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974
Abstract 1. 1.|The self-association of papain at pH 7.8 (Tris buffer; ionic strength, 0.05) has been studied by measuring the weight-average molecular weight (by the Archibald method) and the sedimentation coefficient as a function of protein concentration. 2.
W, Pandit, M S, Rao
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Abstract 1. 1.|The self-association of papain at pH 7.8 (Tris buffer; ionic strength, 0.05) has been studied by measuring the weight-average molecular weight (by the Archibald method) and the sedimentation coefficient as a function of protein concentration. 2.
W, Pandit, M S, Rao
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Development of a radioimmunoassay for papain
Journal of Immunological Methods, 1984Various well-tried radioimmunoassay (RIA) techniques were compared for the quantitation of papain. The evaluation of individual assays was performed by logit-log analysis. The most compatible analytical steps were combined in order to obtain the optimal analytical conditions of the assay. The preferred RIA involves papain labelling with lactoperoxidase,
P, Rauch +4 more
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Benzoylamidoacetonitrile as an inhibitor of papain
Biochimica et Biophysica Acta (BBA) - Enzymology, 19731. 1.|With benzoylarginine ethyl ester as a substrate, benzoylamidoacetonitrile is a strong competitive inhibitor of papain (EC 3.4.4.10) (Ki = 0.14 mM). 2. 2.|The inhibitor is not a poor substrate. 3. 3.|The binding of the inhibitor is governed by groups of pK 3.7 and 8.5, whereas the overall activity (kcat/Km) is governed by groups of pK 4.2 and 8.5.
Sluyterman, L.A.A.E., Wijdenes, J.
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The activation of chymotrypsinogen by papain
Canadian Journal of Biochemistry, 1970Papain has been found to activate bovine chymotrypsinogen A. The optimal conditions for the activation are pH 5.0, temperature 23 °C, and enzyme/substrate ratio 1:20. The chymotrypsin obtained by the papain activation has been isolated. A significant difference between this enzyme and α-chymotrypsin is the absence of the three amino acids (Ser, Gly ...
M C, Shaw, T, Kay, T, Viswanatha
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The activation reaction of papain
Biochimica et Biophysica Acta (BBA) - Enzymology, 19671. 1. Papain is reversibly inactivated in the presence of air and low concentrations of cysteine. This inactivation is enhanced by Fe2+ and Cu2- and is retarded by EDTA. In the absence of cysteine, active papain (separated from the activators by gel filtration) is inactivated at a much lower rate in an almost irreversible manner. 2. 2.
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The reactoin of papain with antipapain
Molecular Immunology, 1965Abstract Rabbit antiserum against papain was prepared and found capable of neutralizing the catalytic activity of enzyme. The precipitin reaction yields two peaks, which are shown to correspond to complexes formed between papain and the intact antibody molecules on the one hand, and with papain-damaged antibodies on the other hand.
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