What question did this study set out to answer?

To determine whether isoleucyl transfer RNA synthetase consists of multiple sub-units or exists as a single continuous polypeptide chain.

February 1, 1970Journal of Biological ChemistryOpen Access

Isoleucyl Transfer Ribonucleic Acid Synthetase Is a Single Polypeptide Chain

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Authors

DAD. ArndtMRC Laboratory of Molecular Biology PBPaul BergUniversité de Bretagne Sud

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Implication

Biophysical analysis demonstrates that isoleucyl transfer RNA synthetase consists of a single polypeptide chain, indicating the enzyme does not dissociate into subunits under denaturing conditions.

Key Points

To determine whether isoleucyl transfer RNA synthetase consists of multiple sub-units or exists as a single continuous polypeptide chain.
Subjected the enzyme to denaturing treatments including reduction, carboxymethylation, oxidation, and reaction with maleic anhydride.
Assessed molecular weight using sodium dodecyl sulfate–polyacrylamide gel electrophoresis and equilibrium centrifugation in 6 M guanidine hydrochloride.
Identified terminal amino acid residues of the oxidized enzyme.
The enzyme does not dissociate into smaller subunits in denaturing solvents following chemical reduction, carboxymethylation, oxidation, or maleic anhydride modification.
Equilibrium centrifugation and gel electrophoresis yield a consistent molecular weight of 114,000 ± 2,000 across native, denatured, and alkylated forms.
Only a single amino-terminal residue, threonine, is detected in the oxidized protein.

Cite This Study

Arndt et al. (1970) studied this question.

synapsesocial.com/papers/6a941b5678fe3e71bd43e339 https://doi.org/10.1016/s0021-9258(18)63381-2

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February 1, 1970Journal of Biological ChemistryOpen Access

Isoleucyl Transfer Ribonucleic Acid Synthetase Is a Single Polypeptide Chain

View Full Paper

Ask AI

Bookmark

Authors

DAD. ArndtMRC Laboratory of Molecular Biology PBPaul BergUniversité de Bretagne Sud

Discussion

Member takes

Implication

Biophysical analysis demonstrates that isoleucyl transfer RNA synthetase consists of a single polypeptide chain, indicating the enzyme does not dissociate into subunits under denaturing conditions.

Key Points

To determine whether isoleucyl transfer RNA synthetase consists of multiple sub-units or exists as a single continuous polypeptide chain.
Subjected the enzyme to denaturing treatments including reduction, carboxymethylation, oxidation, and reaction with maleic anhydride.
Assessed molecular weight using sodium dodecyl sulfate–polyacrylamide gel electrophoresis and equilibrium centrifugation in 6 M guanidine hydrochloride.
Identified terminal amino acid residues of the oxidized enzyme.
The enzyme does not dissociate into smaller subunits in denaturing solvents following chemical reduction, carboxymethylation, oxidation, or maleic anhydride modification.
Equilibrium centrifugation and gel electrophoresis yield a consistent molecular weight of 114,000 ± 2,000 across native, denatured, and alkylated forms.
Only a single amino-terminal residue, threonine, is detected in the oxidized protein.

Cite This Study

Arndt et al. (1970) studied this question.

synapsesocial.com/papers/6a941b5678fe3e71bd43e339 https://doi.org/10.1016/s0021-9258(18)63381-2

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