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Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues.
- F. Tietze
- BiologyAnalytical Biochemistry
- 1 March 1969
Defective sialic acid egress from isolated fibroblast lysosomes of patients with Salla disease.
Normal fibroblasts exposed to N-acetylmannosamine yielded lysosome-rich granular fractions loaded with free (unbound) sialic acid, whose velocity of egress increased with increasing initial loading.…
Sialic acid metabolism in sialuria fibroblasts.
It is concluded that the basic biochemical defect in all known cases of sialuria is a failure of CMP-NeuAc to feedback-inhibit UDP-GlcNAc 2-epimerase and cytidine feeding can lower the intracellular soluble sialic acid concentration of sIALuria cells.
Cystine transport is defective in isolated leukocyte lysosomes from patients with cystinosis.
The activity of a cystine transport system in lysosomes prepared from the leukocytes of patients with cystinosis was found to be deficient. In normal subjects, this system was resistant to…
Molecular-kinetic properties of crystalline trypsinogen.
- F. Tietze
- Biology, ChemistryJournal of Biological Chemistry
- 1 September 1953
Defective cystine exodus from isolated lysosome-rich fractions of cystinotic leucocytes.
Identification of the metabolic defect in sialuria.
- P. Weiss, F. Tietze, W. Gahl, R. Seppala, G. Ashwell
- BiologyJournal of Biological Chemistry
- 25 October 1989
With this technique, the basic defect in sialuria has been identified unequivocally as the loss of feedback control of uridine diphosphate N-acetylglucosamine 2-epimerase by cytidine monophosphates N- acetylneuraminic acid with resultant overproduction of sialic acid.
Glutathionuria: inborn error of metabolism due to tissue deficiency of gamma-glutamyl transpeptidase.
Disulfide reduction in rat liver. I. Evidence for the presence of nonspecific nucleotide-dependent disulfide reductase and GSH-disulfide transhydrogenase activities in the high-speed supernatant…
- F. Tietze
- BiologyArchives of biochemistry and biophysics
- 1 May 1970
Cysteamine depletes cystinotic leucocyte granular fractions of cystine by the mechanism of disulphide interchange.
It is concluded that cysteamine depletes lysosomes of cystine by participating in a thiol-disulphide interchange reaction to produce Cysteine and cysteine-cysteamine mixed disulphides, both of which traverse the cystinotic leucocyte lysOSomal membrane.