The specificity of active-site alkylation by iodoacetic acid in the enzyme thiosulfate sulfurtransferase-Reference-Cited by-同舟云学术

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The specificity of active-site alkylation by iodoacetic acid in the enzyme thiosulfate sulfurtransferase

Published:1982-04 Issue:2 Volume:702 Page:173-177
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Horowitz Paul,Criscimagna Nick L.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference13 articles.

1. Mechanism of Rhodanese Action: Polarographic Studies

2. Effect of Sulfur Binding on Rhodanese Fluorescence

3. Active site peptides of rhodanese

4. Selective reactivity of rhodanese sulfhydryl groups with 5,5′-dithio-bis(2-nitrobenzoic acid)

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1. Chromophore attachment in phycocyanin. Functional amino acids of phycocyanobilin -alpha-phycocyanin lyase and evidence for chromophore binding;FEBS Journal;2006-03

2. Rhodanese Can Partially Refold in Its GroEL−GroES−ADP Complex and Can Be Released to Give a Homogeneous Product;Biochemistry;2002-01-22

3. Active-site sulfhydryl chemistry plays a major role in the misfolding of urea-denatured rhodanese;Journal of Protein Chemistry;2000

4. Active Site Structural Features for Chemically Modified Forms of Rhodanese;Journal of Biological Chemistry;1996-08

5. Reversible folding of rhodanese;Journal of Biological Chemistry;1989-06

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