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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 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 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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Interaction of Papain with Anti-Papain
The Journal of Biochemistry, 1964Y, OKADA +3 more
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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1970
L A, Sluyterman, M J, de Graaf
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L A, Sluyterman, M J, de Graaf
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Non-covalent and covalent immobilization of papain onto Ti3C2 MXene nanosheets
Enzyme and Microbial Technology, 2021Dankui Liao, Jianhua Sun, Lixia Sun
exaly