Generation of an acid-stable and protein-bound persulfide-like residue in alkali or sulfhydryl-treated insulin by a mechanism consonant with the .beta.-elimination hypothesis of disulfide bond lysis-Reference-Cited by-同舟云学术

Generation of an acid-stable and protein-bound persulfide-like residue in alkali or sulfhydryl-treated insulin by a mechanism consonant with the .beta.-elimination hypothesis of disulfide bond lysis

Published:1983-01-04 Issue:1 Volume:22 Page:69-75
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Helmerhorst E.,Stokes G. B.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00270a010

Reference50 articles.

1. Persulfide properties of thiocystine and related trisulfides

2. The preparation and subsequent identification of a dehydroalanyl peptide from alkali-treated oxidised glutathione

3. Insulin: The Structure in the Crystal and its Reflection in Chemistry and Biology by

4. Nε-(dl-2-Amino-2-carboxyethyl)-l-lysine, a New Amino Acid Formed on Alkaline Treatment of Proteins

5. Evidence for an Active Site Persulfide Residue in Rabbit Liver Aldehyde Oxidase

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