Action of Sulfating Agents on Proteins and Model Substances. I. Concentrated Sulfuric Acid

Reitz, H. C.; Ferrel, Robert E.; Fraenkel‐Conrat, H.; Olcott, Henry Steel

doi:10.1021/ja01210a036

Cited by 118 publications

(51 citation statements)

References 2 publications

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“…It is of interest in this regard that not all protein hormones are inactivated by this treatment. Reaction of insulin with sulfuric acid to give insulin sulfate does not destroy biological activity (26).…”

Section: Discussionmentioning

confidence: 99%

In Vitro Thyrotropin-Induced Proteolysis in the Thyroid Gland*

Poffenbarger¹,

Powell²,

Deiss³

1963

J. Clin. Invest.

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Numerous studies, both in vivo and in vitro, have been designed to define the biochemical events influenced by the action of thyrotropin (TSH) on the thyroid gland. In vivo experiments have shown that this hormone stimulates growth of the follicular epithelium, trapping of inorganic iodide, biosynthesis of hormonal iodine, turnover of thyroglobulin, and release of inorganic iodide and hormonal iodine. The latter action has received much attention because of its relevance to the concentration of circulating thyroid hormone and because of the promptness of this response in vivo. De Robertis demonstrated an increase in intrafollicular proteolytic activity after administration of TSH to rats (1). Keating, Rawson, Peacock, and Evans (2) noted loss of radioiodine from the chick thyroid after TSH administration. Similar results have been observed in other laboratory animals (3, 4). The administration of TSH to euthyroid humans also results in prompt release of radioiodine from the thyroid (5-7), occurring 90 minutes after intramuscular inj ection in one study (7).In vitro techniques have permitted investigation in a more rigidly controlled environment. Such observations on the effect of TSH added to thyroid tissue have confirmed the stimulus to the trapping of iodide (8, 9). TSH in vitro has also been shown to enhance certain parameters of intermediary metabolism such as carbon-1 oxidation of glucose (10, 11), phospholipid synthesis (12), oxygen consumption, lipogenesis from labeled glucose, incorporation of inositol into phospholipid (13), and the level of triphosphopyridine nucleotide (14). Few

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Section: Discussionmentioning

confidence: 99%

In Vitro Thyrotropin-Induced Proteolysis in the Thyroid Gland*

Poffenbarger¹,

Powell²,

Deiss³

1963

J. Clin. Invest.

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“…Irrespective of the reagent used, chemical sulfation occurs preferentially at the alcoholic hydroxyl groups of Ser, Thr, and hydroxyPro residues rather than at the phenolic hydroxyl groups of Tyr residues. 87,90,97 Furthermore, in the presence of Cys residues, formation of Cys thiosulfate has also been observed. 87 The undesired sulfation of these residues can sometimes be avoided by a segment synthesis strategy 89 ; however, the use of orthogonally removable protecting groups provides a more general approach to solving this problem.…”

Section: Chemical Sulfation Of Peptidesmentioning

confidence: 93%

“…87,90,97 Furthermore, in the presence of Cys residues, formation of Cys thiosulfate has also been observed. 87 The undesired sulfation of these residues can sometimes be avoided by a segment synthesis strategy 89 ; however, the use of orthogonally removable protecting groups provides a more general approach to solving this problem. 44,45,75,90,93,94 For example, to achieve selective sulfation of specific Tyr residues in peptides synthesized by Fmocbased solid-phase chemistry, Futaki et al introduced the p-(methylsulphinyl)benzyl (Msib) group to protect the sidechains of Ser, Thr, and Tyr and the Msz group to protect the N-a-amino and e-amino groups.…”

Section: Chemical Sulfation Of Peptidesmentioning

confidence: 93%

“…86 Most commonly, Tyr sulfation is achieved by treatment with concentrated sulfuric acid in the cold [43][44][45][87][88][89] or with a complex of sulfur trioxide with either pyridine 38,80,84,[89][90][91][92] or DMF. 75,93,94 With concentrated sulfuric acid, control of reaction temperature and time are crucial to achieve quantitative sulfation and minimize sulfonation as a side reaction.…”

Section: Chemical Sulfation Of Peptidesmentioning

confidence: 99%

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Toward a framework for sulfoproteomics: Synthesis and characterization of sulfotyrosine‐containing peptides

2008

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“…for 11 days, but that later there was slow liberation of amino groups. Reitz et al (28) noted that although appreciable hydrolysis of y-globulin occurred in one weel; a t room I temperature there was only 2-3% hydrolj.sis in 10 days a t 4OC. Work on wool (11) indicated considerable non-ionic combination of sulphate ions with the amino groups to form sulphamates.…”

Section: Introductionmentioning

confidence: 99%

The Action of Sulphuric Acid on Gliadin: With Special Reference to the N-Peptidyl→o-Peptidyl Bond Rearrangement

Ramachandran¹,

McConnell²

1955

Can. J. Chem.

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Treatment of gliadin with sulphuric acid transposes peptide bonds of serine from the amino t o the hydroxyl group. Maximum transposition, 60-70% of the theoretica1, occurs when the protein is treated with anhydrous sulphuric acid a t 0°C. for 35 hr. No rearrangement was detected a t threonine residues. Examination of the peptide materiaI, obtained from the rearranged protein by Elliott's degradation method, indicates apparent "hon~ogeneity". In an alternative scheme for the degradation, nitrous acid deamination of free amino groups was used. The resulting loss in serine content of the protein is direct evidence for the acyl migration of peptide bonds. Incorporation of sulphur and partial disappearance of several amino acids accompany the sulphuric acid treatment. The occurrence of these secondary reactions imposes limitations on the use of sulphuric acid as a reagent for the specific fission of peptide bonds. INTRODUCTIONAttention has recently been directed towards methods which effect fragmentation of protein molecules in a predictable manner. Especially significant is Elliott's procedure for the cleavage of peptide bonds (7, 8, 9) a t the amino groups of the P-hydroxyamino acids, serine and threonine. I t is based on the strong acid-induced N-acyl+O-acyl transformations studied earlier by Bergmann, Brand, and Weinmann (2), Desnuelle and Casal ( 5 ) , and Desnuelle and Bonjour (G), and is briefly outlined in the equations below:. . This N-acyl+O-acyl migration might also occur ~vllere the €-amino groups of f hydroxylysine (26) are linlied in a peptide bond.The treatment of silk fibroin with 97.5% sulphuric acid for three days a t 20°C. (8) caused rearrangelllent in only 66% of the serine residues, the major N-terminal residue detected by the dinitrolluorobenzene method (24) being serine. The non-reactivity of the other serine residues was thought t o result 1AIanuscript received M a y 26, 1955.

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Action of Sulfating Agents on Proteins and Model Substances. I. Concentrated Sulfuric Acid

Cited by 118 publications

References 2 publications

In Vitro Thyrotropin-Induced Proteolysis in the Thyroid Gland*

In Vitro Thyrotropin-Induced Proteolysis in the Thyroid Gland*

Toward a framework for sulfoproteomics: Synthesis and characterization of sulfotyrosine‐containing peptides

The Action of Sulphuric Acid on Gliadin: With Special Reference to the N-Peptidyl→o-Peptidyl Bond Rearrangement

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