Section 42
Chapter 41,072

Principles of enzyme stabilization. V. the possibility of enzyme selfstabilization under the action of potentially reversible intramolecular cross-linkages of different length

Torchilin, V.P.; Maksimenko, A.V.; Smirnov, V.N.; Berezin, I.V.; Martinek, K.

Biochimica et Biophysica Acta 568(1): 1-10


ISSN/ISBN: 0006-3002
PMID: 444535
DOI: 10.1016/0005-2744(79)90267-5
Accession: 041071084

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The denaturing action of guanidine . HCl on modified alpha-chymotrypsin (EC preparations has been studied. The consecutive treatment of alpha-chymotrypsin with N-acetyl-homocysteine thiolactone, 5,5'-dithio-bis-(2-nitrobenzoic acid) and dithiols of HS-(CH2)n-SH type, with n ranging from 4 to 10, leads to enzyme stabilization as a result of protein modification. A greater stabilization effect can be achieved by enriching the protein molecule with groups reactive towards dithiols, after first modifying carboxygroups. In this case dithiol with n=5 forms an intramolecular cross-linkage. If an equimolecular mixture of different dithiols is used for enzyme modification, the enzyme gradually 'selects' 1,5-dithiol for the formation of an intramolecular cross-linkage instead of the initial one-point modification. The use of potentially reversible cross-linkages may be generally employed for the preparation of stabilized water-soluble enzymes via the mechanism of selfstabilization.

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