A New Microdetermination of the Total Quantity of Cysteine Plus Cystine in Protein by Hydrazinolysis

Kuratomi, Kazuoki; Ohno, Ko; Akabori, Shirô

doi:10.1093/oxfordjournals.jbchem.a126743

Cited by 14 publications

(2 citation statements)

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“…It must be pointed out that our figures give a total of 8 (cystine + cysteine) sulphur atoms/ molecule. Tristram (1953) reports one cystine and five cysteine residues from amino acid analysis, giving a total of 7 (cystine + cysteine) sulphur atoms, with which the more recent data of Kuratomi, Ohno & Akabori (1957), who found 7-3, and of Akabori & Fujiwara (1958), who found 6-8, are in substantial agreement. While this discrepancy remains to be resolved, the possibility of low results for cyst(e)ine sulphur in amino acid analyses is recognized (e.g.…”

Section: Hgcl Hgcl2mentioning

confidence: 86%

Physicochemical studies on ovalbumin. 3. The sulphydryl and disulphide contents of ovalbumin and an iodine-modified derivative

Winzor¹,

Creeth²

1962

Biochemical Journal

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Section: Hgcl Hgcl2mentioning

confidence: 86%

Physicochemical studies on ovalbumin. 3. The sulphydryl and disulphide contents of ovalbumin and an iodine-modified derivative

Winzor¹,

Creeth²

1962

Biochemical Journal

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“…The diacetyl monoxide urea method of Wheatley was used by Rendi (510) for the quantitative determination of arginine in nonhydrolyzed proteins. Kuratomi et al (369) used a simplified method of hydrazinolysis for the microdetermination of the total quantity of cysteine plus cystine.…”

Section: New Apparatus and Equipmentmentioning

confidence: 99%

Clinical Chemistry

Kingsley¹

1959

Anal. Chem.

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Disulfide bridges and configuration of human serum albumin. Relationships between viscosity, optical rotatory dispersion and configuration

Jirgensons

Ikenaka

1959

Makromol. Chem.

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The effect of oxidative and reductive cleavage of the disulfide bridges of serum albumin on the viscosity, specific rotation, and rotatory dispersion was investigated. Human serum albumin was oxidized with performic acid a t low temperature. Our data show that oxidized human serum albumin (OHA) prepared in this manner represents an unfolded polyelectrolyte. It could be shown that no peptide bonds were hydrolyzed during the oxidation, and that approximately 90% of all -S-S-bonds were oxidized to -SO,H. From viscosity data (in 4M guanidine thiocyanate) it can be concluded that the SS bonds are important for partial folding, and that some of the -SS-bridges are linking distant parts of the polypeptide chain. This was ascertained also by cleaving the SS bridges by reduction and carboxymethylation. The reduced and carboxymethylated albumin exhibited similar optical rotation and viscosity behavior as the OHA. It was also established that the levorotation does not depend solely on the folding but also on the presence or absence of the SS bonds, i.e. cystine content. Finally, i t was concluded that in the instance of human serum albumin the dispersion constant 1 , is a safer criterion for the estimation of configurational changes than the specific rotation. ZUSAMMENFASSUNG:Die Disulfidbriicken in den Makromolekiilen des Serumalbumins wurden durch oxidative oder reduktive Spaltung gesprengt, und die Viskositat, spezifische Rotation und Rotationsdispersion der Losungen untersucht. Die oxydative Spaltung wurde mit Perameisensaure bei niedriger Temperatur vorgenommen. Durch Aminosaureanalysen und Bestimmung der End-Aminosauren wurde gezeigt, daR 90 yo der Disulfidbriicken -S-Szu -SO,H oxydiert worden waren, und daR die Hauptkette dadurch nicht hydrolytisch abgebaut wurde. Die Losungen des oxydierten Albumins waren hochviskos, die Viskositat erniedrigte sich stark durch Salzzusatz. Vergleichende Viskositatsmessungen in 4 m Guanidinrodanid zeigten, daB die oxydierten Makromolekule ein groaeres Volumen beanspruchen als die Makromolekiile des nicht oxydierten Albumins in demselben Losungsmittel;

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A New Microdetermination of the Total Quantity of Cysteine Plus Cystine in Protein by Hydrazinolysis

Cited by 14 publications

References 0 publications

Physicochemical studies on ovalbumin. 3. The sulphydryl and disulphide contents of ovalbumin and an iodine-modified derivative

Physicochemical studies on ovalbumin. 3. The sulphydryl and disulphide contents of ovalbumin and an iodine-modified derivative

Clinical Chemistry

Disulfide bridges and configuration of human serum albumin. Relationships between viscosity, optical rotatory dispersion and configuration

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