The Lability of the Sulfur in Cystine Derivatives and Its Possible Bearing on the Constitution of Insulin

Brand, Erwin; Sandberg, Marta

doi:10.1016/s0021-9258(18)84494-5

Cited by 35 publications

(3 citation statements)

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“…after several hours, in contrast to the dithio ester (392) (c/. page 63). The action of phenylmagnesium bromide on ethyl thionbenzoate leads to a small yield of benzophenone; hence this reaction must be accompanied by desulfuration (171).…”

Section: Hsch2chch2och2cooh I Shmentioning

confidence: 99%

Cleavage of the Carbon-Sulfur Bond in Divalent Sulfur Compounds.

Tarbell¹,

Harnish²

1951

Chem. Rev.

153

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Section: Hsch2chch2och2cooh I Shmentioning

confidence: 99%

Cleavage of the Carbon-Sulfur Bond in Divalent Sulfur Compounds.

Tarbell¹,

Harnish²

1951

Chem. Rev.

153

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“…This test is specific for –SH containing amino acid, like cysteine, and as mentioned MT is a cysteine‐rich protein. The amino acids containing sulfhydryl group when heated with base, the sulfhydryl, and disulfhydryl group are directly converted to inorganic sulfur, which is confirmed by the black precipitate of PbS (lead sulfide) when adding Pb(C 2 H 3 O 2 ) 2 (lead acetate) [19,20] .…”

Section: Methodsmentioning

confidence: 99%

Expression regulation of chitin‐binding protein and metal‐binding peptide in new Bacillus velezensis: MALDI‐TOF MS/MS analysis

Etemadzadeh

Emtiazi

2021

J Basic Microbiol

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Metallothionein and metal‐binding peptides are small cysteine‐rich proteins produced by different organisms in stress conditions. In this study, the metal‐binding peptide was detected in extracellular proteins of a new Bacillus velezensis strain, isolated from metal contaminated soil, and grown on the lead‐enriched medium, for the first time. The presence of sulfide peptide was assayed by two simple tests (lead sulfide and Ellman's reagent test) for preliminary, and subsequently confirmed using polyacrylamide gel electrophoresis at media with different lead concentrations that the low‐molecular‐weight protein fragments (≈10 kDa) were observed while none were detected in the medium containing sodium chloride or calcium salt. The amino acids of the observed fragments were analyzed by matrix‐assisted laser desorption ionization time‐of‐flight tandem mass spectrometry (MALDI‐TOF MS/MS). Also, the metal adsorption was confirmed using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) by staining with chromium solution. The results showed that the putative sulfide peptide is metallothionein, which is induced in stress conditions. It was interesting that in all SDS profiles, one protein fragment (≈18 kDa) was inhibited in lead‐enriched media. The data from MALDI‐TOF MS/MS analysis showed that this fraction was a chitin‐binding protein whose production was regulated by metal contamination. It is anticipated that these two proteins regulate the toxicity of lead.

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“…The first attempt to produce hypoglycemia by administration of peptides containing sulfur was made in 1926 when Kon and Funk (25) reported that they had obtained no hypoglycemic activity with glutathione in either the oxidized or reduced form. In the same year Brand and Sandberg (39) observed that dialanylcystine and dialanylcystine dianhydride injected intravenously showed no insulin-like properties.…”

Section: Cystine and Cystinyl Peptidesmentioning

confidence: 98%