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

K. I. Shibata; M. Noda; Y. Sawa; T. Watanabe

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

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

Research output: Contribution to journal › Comment/debate › peer-review

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

ASJC Scopus subject areas

Parasitology
Microbiology
Immunology
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Cite this

@article{87b89dd0be08417c9cefb3c4f66a7e20,

title = "Acid phosphatase purified from Mycoplasma fermentans has protein tyrosine phosphatase-like activity",

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.",

author = "Shibata, {K. I.} and M. Noda and Y. Sawa and T. Watanabe",

year = "1994",

month = jan,

day = "1",

language = "English",

volume = "62",

pages = "313--315",

journal = "Infection and Immunity",

issn = "0019-9567",

publisher = "American Society for Microbiology",

number = "1",

}

TY - JOUR

T1 - Acid phosphatase purified from Mycoplasma fermentans has protein tyrosine phosphatase-like activity

AU - Shibata, K. I.

AU - Noda, M.

AU - Sawa, Y.

AU - Watanabe, T.

PY - 1994/1/1

Y1 - 1994/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0028115739&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028115739&partnerID=8YFLogxK

M3 - Comment/debate

C2 - 7505261

AN - SCOPUS:0028115739

VL - 62

SP - 313

EP - 315

JO - Infection and Immunity

JF - Infection and Immunity

SN - 0019-9567

IS - 1

ER -

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

Abstract

ASJC Scopus subject areas

UN SDGs

Other files and links

Fingerprint

Cite this