Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Cysteine metabolism  (4)
  • Sulfate formation  (3)
  • 3-Mercaptopyruvate pathway  (2)
  • 1
    ISSN: 1438-2199
    Keywords: Amino acids ; Cysteine metabolism ; 3-Mercaptopyruvate pathway ; Cysteine transamination ; 3-Mercaptolactate-cysteine mixed disulfide ; Sulfate formation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have studied the transamination pathway (3-mercaptopyruvate pathway) ofl-cysteine metabolism in rats. Characterization of cysteine aminotransferase (EC 2.6.1.3) from liver indicated that the transamination, the first reaction of this pathway, was catalyzed by aspartate aminotransferase (EC 2.6.1.1). 3-Mercaptopyruvate, the product of the transamination, may be metabolized through two routes. The initial reactions of these routes are reduction and transsulfuration, and the final metabolites are 3-mercaptolactate-cysteine mixed disulfide [S-(2-hydroxy-2-carboxyethylthio)cysteine, HCETC] and inorganic sulfate, respectively. The study using anti-lactate dehydrogenase antiserum proved that the enzyme catalyzing the reduction of 3-mercaptopyruvate was lactate dehydrogenase (EC 1.1.1.27). Formation of HCETC was shown to depend on low 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) activity. Results were discussed in relation to HCETC excretion in normal human subjects and patients with 3-mercaptolactate-cysteine disulfiduria. Incubation of liver mitochondria withl-cysteine, 2-oxoglutarate and glutathione resulted in the formation of sulfate and thiosulfate, indicating that thiosulfate was formed by transsulfuration of 3-mercaptopyruvate and finally metabolized to sulfate.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1438-2199
    Keywords: Amino acids ; l-2-Oxothiazolidine-4-carboxylate ; Cysteine precursor ; Cysteine metabolism ; Sulfate ; Taurine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Five mmol ofl-2-oxothiazolidine-4-carboxylate (OTC)/kg of body weight was administered into the stomach of rats, and cysteine levels in tissues and sulfate and taurine excreted in the urine were determined. The cysteine (plus cystine expressed as cysteine) concentration in the liver increased to 170–200% of the original level at 30 min and that in the blood to 160% at 60 min after the OTC administration. These high levels were maintained until 8 h after the administration and decreased gradually thereafter. Excretion of sulfate and taurine increased after the OTC administration and the increase corresponded to 26% and 15%, respectively, of the OTC administered. These findings suggest that at least about 40% of the OTC administered into the stomach was taken up and converted to cysteine, which was metabolized to sulfate and taurine.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1438-2199
    Keywords: Amino acids ; Cysteine metabolism ; MP pathway ; Sulfate formation ; (Aminooxy)acetate ; Rat liver mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The effect of (aminooxy)acetate, an inhibitor of aminotransferases, on the sulfate formation froml-cysteine andl-cysteinesulfinate in rat liver mitochondria was studied. Incubation of 10 mMl-cysteine with rat liver mitochondria at 37°C in the presence of 10 mM 2-oxoglutarate and 10 mM glutathione resulted in the formation of 4.60 and 1.52µmol of sulfate and thiosulfate, respectively, per 60 min per mitochondria obtained from 1 g of liver. Under the same conditions sulfate formation froml-cysteinesulfinate was 24.96µmol, but thiosulfate was not formed. The addition of (aminooxy)acetate at 2 mM or more completely inhibited the sulfate and thiosulfate formation froml-cysteine and the sulfate formation froml-cysteinesulfinate. These findings support our previous conclusion that cysteine transamination and 3-mercaptopyruvate pathway (MP pathway) are involved in the sulfate formation froml-cysteine in rat liver mitochondria (Ubuka et al., 1992).
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1438-2199
    Keywords: Amino acids ; Cysteine metabolism ; 3-Mercaptopyruvate pathway ; Sulfate formation ; Mitochondria ; Glutathione
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have studied the 3-mercaptopyruvate pathway (transamination pathway) ofl-cysteine metabolism in rat liver mitochondria.l-Cysteine and other substrates at 10 mM concentration were incubated with mitochondrial fraction at pH 8.4, and sulfate and thiosulfate were determined by ion chromatography. Whenl-cysteine alone was incubated, sulfate formed was 0.7µmol per mitochondria from one g of liver per 60 min. Addition of 2-oxoglutarate and GSH resulted in more than 3-fold increase in sulfate formation, and thiosulfate was formed besides sulfate. The sum (A + 2B) of sulfate (A) and thiosulfate (B) formed was approximately 7-times that withl-cysteine alone. Incubation with 3-mercaptopyruvate resulted in sulfate and thiosulfate formation, and sulfate was formed with thiosulfate. These reactions were stimulated with glutathione. Sulfate formation froml-cysteinesulfinate and 2-oxoglutarate was not enhanced by glutathione and thiosulfate was not formed. These findings indicate thatl-cysteine was metabolized and sulfate was formed through 3-mercaptopyruvate pathway in mitochondria.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...