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Science 5 November 1965:
Vol. 150. no. 3697, pp. 758 - 760
DOI: 10.1126/science.150.3697.758
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Articles

Papain Membrane on a Collodion Matrix: Preparation and Enzymic Behavior

R. Goldman 1, H. I. Silman 1, S. R. Caplan 1, O. Kedem 1, and E. Katchalski 1

1 Department of Biophysics and Polymer Research, Weizmann Institute of Science, Rehovoth, Israel

A stable papain membrane has been prepared on a collodion matrix by absorbing papain in a collodion membrane and then cross-linking the papain with bisdiazobenzidine 3,3'-disulfonic acid. The pH-dependence of the activity of the enzyme membrane on the low-molecular-weight substrate, benzoylarginine ethyl ester, was found to differ from that of crystalline papain; the activity was low in the neutral pH range where the native enzyme has its optimum and high at alkaline pH. This anomalous behavior is due to a lowering of the local pH within the membrane as a result of the release of acid by the enzymic hydrolysis of the ester substrate.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Trypsin and Papain Covalently Coupled to Porous Glass: Preparation and Characterization.
H. H. Weetall (1969)
Science 166, 615-617
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Electrical Phenomena Associated with the Activity of the Membrane-Bound Acetylcholinesterase.
T. Podleski and J. P. Changeux (1967)
Science 157, 1579-1581
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