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Substrate specificity of monomeric and dimeric α‐sarcin
Author(s) -
Cheung Jin-I.,
Wang Yuh-Ru,
Lin Alan
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00404-8
Subject(s) - ribonuclease , deoxyribonuclease , ribosome , rna , biochemistry , monomer , gel electrophoresis , chemistry , biology , microbiology and biotechnology , enzyme , gene , organic chemistry , polymer
The substrate specificity of monomeric and dimeric forms of α‐sarcin was investigated by membrane blotting procedures. Dimeric α‐sarcin fails to inactivate ribosomes as well as to hydrolyze mini‐stem‐loop RNA, whereas monomeric α‐sarcin catalyzes both substrates. Both monomeric and dimeric α‐sarcin are effective ribonucleases that are displayed by in situ RNA‐impregnated gel electrophoresis. The same purine base specificity was detected for both dimeric and monomeric forms. α‐Sarcin is also an effective deoxyribonuclease to supercoiled DNA. The action of α‐sarcin as deoxyribonuclease and ribonuclease is inhibited by the presence of SDS (3.5 × 10 −6 M); the inhibition on ribonuclease, but not on deoxyribonuclease, is reversible if the proteins are renatured.