Characterization of an ecto-phosphatase activity in the human parasiteTrichomonas vaginalis
β Scribed by J. de Jesus; T. Podlyska; A. Hampshire; C. Lopes; M. Vannier-Santos; J. Meyer-Fernandes
- Publisher
- Springer-Verlag
- Year
- 2002
- Tongue
- English
- Weight
- 265 KB
- Volume
- 88
- Category
- Article
- ISSN
- 1432-1955
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract The physiological function of alkaline phosphatase (ALP) remains controversial. It was recently suggested that this membraneβbound enzyme has a role in the modulation of transmembranar transport systems into hepatocytes and Cacoβ2 cells. ALP activity expressed on the apical surface of b
## Abstract Alkaline phosphatase (ALP) refers to a group of nonspecific phosphomonoesterases located primarily in cell plasma membrane. It has been described in different cell lines that ectoβALP is directly or indirectly involved in the modulation of organic cation transport. We aimed to investiga
A preliminary characterization of the protein phosphotyrosine phosphatase (PT-Pase) activity in human peripheral blood lymphocytes (PBL) has been made using two tyrosine-containing peptides and the epidermal growth factor receptor from A-431 cells as substrates. High PTPase activity with a pH optimu
The isolated brush border membrane of the tapeworm, Hymenolepis diminuta, hydrolyzes p-nitrophenyl phosphate over a broad pH range. Acid phosphatase activity (pH optimum at 4.0) is inhibited specifically by sodium dodecyl sulfate (SDS) and NaF, while the alkaline phosphatase activity (pH optimum at