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The Behavior of Cleavable Crosslinking Reagents Based on the Disulfide Group
Author(s) -
Wang Kuan,
Richards Frederic M.
Publication year - 1974
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.197400030
Subject(s) - chemistry , reagent , aldolase a , disulfide bond , bifunctional , sodium dodecyl sulfate , thiol , protein disulfide isomerase , combinatorial chemistry , chromatography , organic chemistry , biochemistry , enzyme , catalysis
4,4′‐Bisphenyldiazonium disulfide fluoroborate and dimethyl‐3,3′‐dithiobispropionimidate dihydrochloride were synthesized and tested as reversible cross‐linking reagents. Rabbit muscle aldolase, human hemoglobin and human erythrocyte membrane proteins can be successfully crosslinked by these reagents. The crosslinked products can be cleaved into their components in high yield by thiols, under mild conditions. A simple diagonal sodium dodecyl sulfate gel electrophoresis technique was developed to identify electrophoretically the components of crosslinked products. The application and possible complications of bifunctional reagents containing disulfide bonds are discussed.