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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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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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Inhibition of papain by isothiocyanates
Biochimica et Biophysica Acta (BBA) - Enzymology, 1976During the tapping of papaya latex for papain (EC 3.4.22.2), benzyl isothiocyanate is enzymatically produced from benzylglucosinolate, a major component of the latex fluid. Benzyl isothiocyanate inhibits papain hydrolysis of alpha-N-benzoyl-L-arginine ethyl ester (Bz-Arg-OEt).
C S, Tang, W J, Tang
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The mechanism of the activation of papain
Biochemical and Biophysical Research Communications, 1969Abstract The predominant form of inactive papain prepared by the method of Kimmel and Smith (1) is shown to be a mixed disulfide formed between a sulfhydryl group on the enzyme and cysteine. Reduction or other nucleophilic cleavage of this bond frees the active thiol of papain and stoichiometric amounts of free cysteine or cysteine whose sulfur atom ...
I B, Klein, J F, Kirsch
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The hydrolysis of lipovitellin by papain
Archives of Biochemistry and Biophysics, 1963Abstract The effect of papain on lipovitellin from hen's egg yolk has been investigated. In one experiment, the mixture from the enzymic hydrolyzate was separated on Sephadex G-75 into two components, A 1 and B 1 . Component A 1 contained 84% of the lipids and 12% of the protein from the lipovitellin.
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Journal of Applied Physiology, 1976
Sera from seven animal species (rat, cow, cat, dog, human, rabbit, and hamster) were tested and found to inhibit the papain-catalyzed hydrolysis of alpha-N-benzoyl-L-arginine-p-nitroaniline-HCl (L-BAPA). The relative concentration of inhibitor in each serum sample was expressed in terms of its papain inhibitory capacity (PIC) defined as the number of ...
M J, Fisher +3 more
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Sera from seven animal species (rat, cow, cat, dog, human, rabbit, and hamster) were tested and found to inhibit the papain-catalyzed hydrolysis of alpha-N-benzoyl-L-arginine-p-nitroaniline-HCl (L-BAPA). The relative concentration of inhibitor in each serum sample was expressed in terms of its papain inhibitory capacity (PIC) defined as the number of ...
M J, Fisher +3 more
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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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ULTRAVIOLET INACTIVATION OF PAPAIN*
Photochemistry and Photobiology, 1975Abstract— Flash photolysis transient spectra (Λ > 250 nm) of aqueous papain show that the initial products are the neutral tryptophan radical Tip (Λmax 510 nm), the tryptophan triplet state 3Trp (Λm., 460nm), the disulfide bridge electron adduct –ṠS‐— (Λmax 420nm) and the hydrated electron eaq‐.
J F, Baugher, L I, Grossweiner
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