Acid phosphatase purified from Mycoplasma fermentans has protein tyrosine phosphatase-like activity

K. I. Shibata, M. Noda, Yoshihiko Sawa, T. Watanabe

Research output: Contribution to journalComment/debate

13 Citations (Scopus)

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 languageEnglish
Pages (from-to)313-315
Number of pages3
JournalInfection and Immunity
Volume62
Issue number1
Publication statusPublished - 1994
Externally publishedYes

Fingerprint

Mycoplasma fermentans
Protein Tyrosine Phosphatases
Acid Phosphatase
Phosphotyrosine
Vanadates
Mycoplasma
Muramidase
Phosphoric Monoester Hydrolases
Sodium
Peptides
Raytide

ASJC Scopus subject areas

  • Immunology

Cite this

Acid phosphatase purified from Mycoplasma fermentans has protein tyrosine phosphatase-like activity. / Shibata, K. I.; Noda, M.; Sawa, Yoshihiko; Watanabe, T.

In: Infection and Immunity, Vol. 62, No. 1, 1994, p. 313-315.

Research output: Contribution to journalComment/debate

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