نتایج جستجو برای: purple acid phosphatase

تعداد نتایج: 790751  

Journal: :Biochemistry 2004
Paul V Bernhardt Gerhard Schenk Gregory J Wilson

Cyclic voltammetry of the non-heme diiron enzyme porcine purple acid phosphatase (uteroferrin, Uf) has been reported for the first time. Totally reversible one-electron oxidation responses (FeIII-FeII --> FeII-FeIII) are seen both in the absence and in the presence of weak competitive inhibitors phosphate and arsenate, and dissociation constants of these oxoanion complexes formed with uteroferr...

2016
Renshan Zhang Xiaoqian Guan Yee-Song Law Feng Sun Shuai Chen Kam Bo Wong Boon Leong Lim

Arabidopsis thaliana purple acid phosphatase 2 (AtPAP2) is the only phosphatase that is dual-targeted to both chloroplasts and mitochondria. Like Toc33/34 of the TOC and Tom 20 of the TOM, AtPAP2 is anchored to the outer membranes of chloroplasts and mitochondria via a hydrophobic C-terminal motif. AtPAP2 on the mitochondria was previously shown to recognize the presequences of several nuclear-...

2011
Fei Dai Long Qiu Lingzhen Ye Dezhi Wu Meixue Zhou Guoping Zhang

BACKGROUND Endogenous phytase plays a crucial role in phytate degradation and is thus closely related to nutrient efficiency in barley products. The understanding of genetic information of phytase in barley can provide a useful tool for breeding new barley varieties with high phytase activity. METHODOLOGY/PRINCIPAL FINDINGS Quantitative trait loci (QTL) analysis for phytase activity was condu...

Journal: :The Journal of biological chemistry 2001
G Schenk C L Boutchard L E Carrington C J Noble B Moubaraki K S Murray J de Jersey G R Hanson S Hamilton

A purple acid phosphatase from sweet potato is the first reported example of a protein containing an enzymatically active binuclear Fe-Mn center. Multifield saturation magnetization data over a temperature range of 2 to 200 K indicates that this center is strongly antiferromagnetically coupled. Metal ion analysis shows an excess of iron over manganese. Low temperature EPR spectra reveal only re...

Journal: :The Journal of biological chemistry 1986
G A Baumbach C M Ketcham D E Richardson F W Bazer R M Roberts

A pink, high molecular weight form of uteroferrin (Uf) has been isolated from uterine secretions and allantoic fluid of pigs. This protein fraction (denoted FIII) which is relatively stable under physiological conditions of pH, ionic strength, and temperature has a molecular weight of about 80,000, a value approximately twice that of purple Uf (Mr approximately 35,000) isolated from a separate ...

Journal: :The Journal of biological chemistry 2003
Carlo Zambonelli Mary F Roberts

Recombinant phospholipase D (PLD) from Streptomyces chromofuscus (scPLD) has been characterized using colorimetric assays, spectroscopic investigations, and site-directed mutagenesis. scPLD, which shows phosphodiesterase activity toward a wide variety of phospholipids and phosphatase activity toward p-nitrophenyl phosphate, exhibits a visible absorption band with lambda(max) at 570 nm. Metal io...

Journal: :Inorganic chemistry 2010
Fergal Coleman Michael J Hynes Andrea Erxleben

The effects of a series of Ga(III) complexes with tripodal ligands on the hydrolysis rate of the activated phosphate diester bis(2,4-dinitrophenyl)phosphate (BDNPP) have been investigated. In particular, the influence of the nature of the ligand donor sites on the reactivity of Ga(III) which represents a mimic of the Fe(III) ion in purple acid phosphatase has been evaluated. It has been shown t...

Journal: :Journal of bacteriology 1991
S Au K L Roy R G von Tigerstrom

Lysobacter enzymogenes produces an alkaline phosphatase which is secreted into the medium. The gene for the enzyme (phoA) was isolated from a recombinant lambda library. It was identified within a 4.4-kb EcoRI-BamH1 fragment, and its sequence was determined by the chain termination method. The structural gene consists of an open reading frame which encodes a 539-amino-acid protein with a 29-res...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید