Alkaline phosphatase from the Antarctic strain TAB5. Properties and psychrophilic adaptations.
about
Cold and Hot Extremozymes: Industrial Relevance and Current TrendsOptimization to low temperature activity in psychrophilic enzymesCoordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatasesCloning, sequences, and characterization of two chitinase genes from the Antarctic Arthrobacter sp. strain TAD20: isolation and partial characterization of the enzymes.A novel psychrophilic alkaline phosphatase from the metagenome of tidal flat sediments.Alkaline phosphatase from the hyperthermophilic bacterium T. maritima requires cobalt for activity.Microdiversity of extracellular enzyme genes among sequenced prokaryotic genomesPsychrophilic enzymes: from folding to function and biotechnology.Structural characteristics of alkaline phosphatase from the moderately halophilic bacterium Halomonas sp. 593.Biotechnological applications of psychrophiles.Biotechnological uses of enzymes from psychrophiles.Antarctic DNA moving forward: genomic plasticity and biotechnological potential.Engineering the properties of a cold active enzyme through rational redesign of the active site.Recombinant production and characterization of a highly active alkaline phosphatase from marine bacterium Cobetia marina.Characterization of a highly thermostable alkaline phosphatase from the euryarchaeon Pyrococcus abyssi.Direct amplification of single-stranded DNA for pyrosequencing using linear-after-the-exponential (LATE)-PCR.Establishing the stability and reversibility of protein pyrophosphorylation with synthetic peptides.Identification and characterization of yeasts isolated from sedimentary rocks of Union Glacier at the Antarctica.Exploring the role of a glycine cluster in cold adaptation of an alkaline phosphatase.Effects of replacing active site residues in a cold-active alkaline phosphatase with those found in its mesophilic counterpart from Escherichia coli.2'-(R)-Fluorinated mC, hmC, fC and caC triphosphates are substrates for DNA polymerases and TET-enzymes.Cloning and expression of a highly active recombinant alkaline phosphatase from psychrotrophic Cobetia marina.Altering of the metal specificity of Escherichia coli alkaline phosphatase.
P2860
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P2860
Alkaline phosphatase from the Antarctic strain TAB5. Properties and psychrophilic adaptations.
description
2000 nî lūn-bûn
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2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
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2000年论文
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name
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@ast
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@en
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@nl
type
label
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@ast
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@en
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@nl
prefLabel
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@ast
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@en
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@nl
P2093
P2860
P1433
P1476
Alkaline phosphatase from the ...... and psychrophilic adaptations.
@en
P2093
K Mavromatis
M Kokkinidis
M Tzanodaskalaki
V Bouriotis
P2860
P304
P356
10.1046/J.1432-1327.2000.01127.X
P407
P577
2000-02-01T00:00:00Z