Effect of the urea-urease system and the carbonate ion on the activities of lactate dehydrogenase isoenzymes.

@article{Fujimoto1970EffectOT,
  title={Effect of the urea-urease system and the carbonate ion on the activities of lactate dehydrogenase isoenzymes.},
  author={Yasuo Fujimoto and John Henry Wilkinson},
  journal={Biochimica et biophysica acta},
  year={1970},
  volume={206 1},
  pages={
          38-45
        }
}
6 Citations

The inhibitory effect of the urea-urease system on human tissue alkaline phosphatases.

Hormonal regulation of acid phosphatase release by osteoclasts disaggregated from neonatal rat bone

Osteoclasts disaggregated from neonatal rat long bones and incubated on plastic or glass substrates were found to release a considerable proportion of tartrate‐resistant acid phosphatase into culture supernatants, suggesting a central role for acid hydrolase secretion in osteoclastic bone resorption.

Zur Lactatdehydrogenase-Isoenzymverteilung im menschlichen Knorpel

  • G. WeselohA. Fiesselmann
  • Chemistry, Philosophy
    Archiv für orthopädische und Unfall-Chirurgie, mit besonderer Berücksichtigung der Frakturenlehre und der orthopädisch-chirurgischen Technik
  • 2004
SummaryThe analysis of the lactatdehydrogenase(LDH)-isoenzym patterns in normal human cartilage will be of valuable help in the interpretation of enzymological data in cases of pathological joint

Middle molecule hypothesis and short dialysis

Uremia is characterized by the retention of numerous substances normally metabolized or excreted by the kidneys. Its pathogenesis has thus always been strongly linked to the concept of the toxicity

References

SHOWING 1-10 OF 12 REFERENCES

ORGAN SPECIFICITY AND LACTATE-DEHYDROGENASE ACTIVITY. DIFFERENTIAL INHIBITION BY UREA AND RELATED COMPOUNDS.

The effect of urea on the lactate-dehydrogenase activities of human-heart and -liver tissue extracts and on crystalline ox- heart and rabbit-muscle enzyme have been determined and an inverse relationship between sensitivity to urea inhibition and electrophoretic mobility is shown.

Lactate dehydrogenase activity in high pyruvate concentrations modified by urea.

  • A. KonttinenS. Lindy
  • Chemistry
    Clinica chimica acta; international journal of clinical chemistry
  • 1967

Lactic dehydrogenase. V. Inhibition by oxamate and by oxalate.

Measurements indicate that for beef heart muscle lactic dehydrogenase oxalate also competes with lactate, and a tentative explanation of the phenomena which are observed in oxamate inhibition is formed.

Nature of the inhibitors of lactate dehydrogenase in uremic dialysates.

It is concluded that some other factor is involved in the first peak, since the inhibitory effects did not correlate with the urea content before and after dialysis, and is considered unlikely to account for the action of peak 3.

Urea and oxalate inhibition of the serum lactate dehydrogenase

The use of oxalate or urea is recommended as an aid in the enzymatic diagnosis of heart and liver disease, especially when the results of other enzyme tests are equivocal.

The determination of lactate dehydrogenase isoenzymes in normal human muscle and other tissues.

  • A. Emery
  • Biology
    The Biochemical journal
  • 1967
With increasing age there was a significant decrease in the total amount of lactate dehydrogenase and the amount of LDH-M in skeletal muscle, which could not be accounted for by the replacement of functioning muscle tissue by fibrous connective tissue.

Alpha-hydroxybutyrate dehydrogenase activity in sex-linked muscular dystrophy

Muscle from two unaffected members of the same family also exhibited high ratios, indicating the presence of the electrophoretically fast LD isoenzymes, and this was confirmed by acrylamide-gel electrophoresis.

A convenient apparatus for vertical gel electrophoresis.

An apparatus is described incorporating gel mold, electrode chambers, and direct-contact cooling plates. It eliminates several steps in preparing and handling the gel, and permits use of either rigid