Abstract
Acid phosphatase purified from Mycoplasma fermentans dephosphorylated phosphotyrosine-containing lysozyme and Raytide, a peptide substrate for protein tyrosine phosphatases. The optimum pH for Raytide was about 5.5. Raytide phosphatase activity was inhibited by potassium fluoride, sodium molybdate, and sodium orthovanadate and was found to exist in some mycoplasmas.
| Original language | English |
|---|---|
| Pages (from-to) | 313-315 |
| Number of pages | 3 |
| Journal | Infection and Immunity |
| Volume | 62 |
| Issue number | 1 |
| Publication status | Published - Jan 1 1994 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Parasitology
- Microbiology
- Immunology
- Infectious Diseases
Cite this
Shibata, K. I., Noda, M., Sawa, Y., & Watanabe, T. (1994). Acid phosphatase purified from Mycoplasma fermentans has protein tyrosine phosphatase-like activity. Infection and Immunity, 62(1), 313-315.