Characterization of human tissue carnosinase.

@article{Lenney1985CharacterizationOH,
  title={Characterization of human tissue carnosinase.},
  author={J. F. Lenney and S C Peppers and C M Kucera-Orallo and Robert P. George},
  journal={The Biochemical journal},
  year={1985},
  volume={228 3},
  pages={653-60}
}
Human tissue carnosinase (EC 3.4.13.3) had optimum activity at pH9.5 and was a cysteine peptidase, being activated by dithiothreitol and inhibited by p-hydroxymercuribenzoate. By optimizing assay conditions, the activity per g of tissue was increased 10-fold compared with values in the literature. The enzyme was present in every human tissue assayed and was entirely different from serum carnosinase. Highly purified tissue carnosinase had a broader specificity than hog kidney carnosinase… CONTINUE READING

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