ACID-PHOSPHATASE PURIFIED FROM MYCOPLASMA-FERMENTANS HAS PROTEIN-TYROSINE PHOSPHATASE-LIKE ACTIVITY

被引：17
|
作者：
SHIBATA, KI [1 ]
NODA, M [1 ]
SAWA, Y [1 ]
WATANABE, T [1 ]
机构：
[1] HOKKAIDO UNIV,SCH DENT,DEPT OPERAT DENT,KITA KU,SAPPORO,HOKKAIDO 060,JAPAN
来源：
INFECTION AND IMMUNITY | 1994年 / 62卷 / 01期
关键词：
D O I：
10.1128/IAI.62.1.313-315.1994
中图分类号：
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号：
100102 ;
摘要：
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.
引用
收藏
页码：313 / 315
页数：3
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