Results 31 to 40 of about 3,329,624 (262)

Isolation and characterization of purple acid phosphatase gene during seedling development in mungbean

open access: yes, 2013
Purple acid phosphatases (PAPs), which are normally found in plant tissues, can hydrolyze a broad spectrum of phosphate esters. In this study, a mungbean [Vigna radiata (L.) Wilczek cv.
A. Wongkaew, P. Srinives, S. Nakasathien
core   +1 more source

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

open access: yesFEBS Letters, EarlyView.
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley   +1 more source

Surface phosphatase activities on roots of Pakistani wheat cultivars [PDF]

open access: yes, 1994
A study of the surface phosphatase activity of different wheat cuhivar roots was carried out, using two substrates, p-nitrophenyl phosphate (pNPP) and 4- methylumbellferyl phosphate (4-MUP), and different pH values ranging from 3 to 10.0.
Chandio, G. Mustafa
core  

Acid phosphatase assay.

open access: yes, 2013
Acid phosphatase activity was determined from whole cell lysates of F. tularensis acid phosphatase mutants by a fluorometric method using DiF-MUP as the substrate. The data are presented as percent of wild type phosphatase activity.
Kristi L. Strandberg (283144)   +4 more
core   +1 more source

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

open access: yesFEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens   +8 more
wiley   +1 more source

Cell-bound phosphatase activity in cotton (gossypium hirsutum L.) roots [PDF]

open access: yes, 1995
A study was made of phosphorus nutrition in cotton cultivars derived from Pakistan with particular reference to phosphatase activity. Cultivars used were Qalandri, Rehmani, Reshami and TH-3/83; Qalandri was used for most of the phosphatase ...
Baloch, Gul Muhammad M.
core  

Acid phosphatases and ribonucleases from Dactylis glomerata seeds. I. Chromatographic and electrophoretic heterogeneity of the enzymes

open access: yesActa Societatis Botanicorum Poloniae, 2015
Acid phosphatase and ribonuclease extracted with 0.1 M sodium acetate buffer, pH 5.1 from Dactylis glomerata seeds, and partially purified by means of 70% ethanol precipitation showed electrophoretic and Chromatographic heterogeneity.
Eleonora Wieczorek   +2 more
doaj   +1 more source

Reconstructing enzyme evolution by protein engineering

open access: yesFEBS Letters, EarlyView.
Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler   +2 more
wiley   +1 more source

Inhibition of Acid Phosphatase Enzyme Activity in the Presence of Noncrystalline Calcium Phosphate and Nanocrystalline Calcium Apatite: a Preliminary Study [PDF]

open access: yes, 2009
*Background* Our bones are remodelled repeatedly during life. A new and “healthy” bone tissue replaces the old one. Accordingly, the bone degrading cells, the osteoclasts, prefer old and fatigued bone.
Yassen Pekounov
core  

Acid phosphatase from stored Poa pratensis caryopses and its ability for binding to lectins

open access: yesActa Societatis Botanicorum Poloniae, 2014
The effect of the storage period of Poa pratensis caryopses on acid phosphatase activity and on the ability of this enzyme to interact with lectins has been studied.
Irena Lorenc-Kubis   +1 more
doaj   +1 more source

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