Results 181 to 190 of about 51,627 (231)
Some of the next articles are maybe not open access.
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
openaire +2 more sources
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
openaire +2 more sources
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.
openaire +2 more sources
Abstract Papain possesses several regions of internal homology and similar shape. The enzyme probably formed through a series of gene doublings.
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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.
openaire +2 more sources
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
openaire +2 more sources
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.
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources