475941
Myokinase, Yeast
Synonim(y):
Myokinase, Yeast, Adenylate Kinase, ATP:AMP Phosphotransferase
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About This Item
Polecane produkty
Postać
lyophilized
Poziom jakości
aktywność właściwa
≥10 units/mg solid
≥200 U/mg
producent / nazwa handlowa
Calbiochem®
warunki przechowywania
OK to freeze
desiccated (hygroscopic)
pI
5.7
rozpuszczalność
water: 1 mg/mL
obecność zanieczyszczeń
ATPase ≤0.01%
Phosphoglycerate kinase ≤0.1%
Warunki transportu
wet ice
temp. przechowywania
−20°C
Opis ogólny
Native, yeast myokinase. Myokinase reversibly transfers phosphate from ATP to AMP, thus forming two molecules of ADP. The enzyme is specific for adenine nucleotides and catalyzes the reaction only in the presence of a divalent metal ion (e.g. Mg2+, Ca2+, Co2+, Mn2+, or Ni2+).
Native, yeast myokinase. Myokinase reversibly transfers phosphate from ATP to AMP, thus forming two molecules of ADP. The enzyme is specific for adenine nucleotides and catalyzes the reaction only in the presence of a divalent metal ion (e.g. Mg2+, Ca2+, Co2+, Mn2+, or Ni2+).
Note: 1 KU = 1000 units.
Ostrzeżenie
Toxicity: Standard Handling (A)
Definicja jednostki
One unit is defined as the amount of enzyme that will convert 1.0 µmol ATP and 1.0 µmol AMP to 2 µmol ADP per min at 25°C, pH 7.5. Note: 1 KU = 1000 units.
Postać fizyczna
Lyophilized from potassium phosphate buffer.
Rekonstytucja
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Inne uwagi
Makarchikov, A.F., et al. 2002. Biochem. Biophys. Acta.1592, 117.
Schricker, R., et al. 2002. J. Biol. Chem.277, 28757.
Magdolen, V., et al. 1987. Curr. Genet.12, 405.
Tomasselli, A.G., et al. 1986. Eur. J. Biochem.155, 111.
Ito, Y., et al. 1980. Eur. J. Biochem.105, 85.
Schricker, R., et al. 2002. J. Biol. Chem.277, 28757.
Magdolen, V., et al. 1987. Curr. Genet.12, 405.
Tomasselli, A.G., et al. 1986. Eur. J. Biochem.155, 111.
Ito, Y., et al. 1980. Eur. J. Biochem.105, 85.
Informacje prawne
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Kod klasy składowania
13 - Non Combustible Solids
Klasa zagrożenia wodnego (WGK)
WGK 3
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Certyfikaty analizy (CoA)
Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
V Magdolen et al.
Current genetics, 12(6), 405-411 (1987-01-01)
The structural gene for yeast adenylate kinase (AKY) has been isolated and analyzed with respect to its nucleotide sequence. Southern and northern analyses imply that the gene is single copy and is transcribed into an mRNA of about 1,100 bases.
Y Ito et al.
European journal of biochemistry, 105(1), 85-92 (1980-03-01)
An improved homogeneous preparation of adenylate kinase (ATP:AMP phosphotransferase, ATP + AMP in equilibrium 2 ADP) from baker's yeast was attained by extraction using ethyl acetate and successive column chromatography on Affi-Gel blue, Sephadex G-100, phosphocellulose and Sephacryl S-200. The
A G Tomasselli et al.
European journal of biochemistry, 155(1), 111-119 (1986-02-17)
The complete amino acid sequence of cytosolic adenylate kinase (MgATP + AMP----MgADP + ADP) from baker's yeast has been determined. Tryptic and clostripaic cleavage of the protein yielded 27 and 10 fragments, respectively. They were sequenced with either a solid-phase
Roland Schricker et al.
The Journal of biological chemistry, 277(32), 28757-28764 (2002-06-05)
Yeast adenylate kinase (Aky2p, Adk1p) occurs simultaneously in cytoplasm and mitochondrial intermembrane space. It has no cleavable mitochondrial targeting sequence, and the signal for mitochondrial import and submitochondrial sorting is largely unknown. The extreme N terminus of Aky2p is able
Alexander F Makarchikov et al.
Biochimica et biophysica acta, 1592(2), 117-121 (2002-10-16)
Thiamine triphosphate (ThTP) is found at low concentrations in most animal tissues and it may act as a phosphate donor for the phosphorylation of proteins, suggesting a potential role in cell signaling. Two mechanisms have been proposed for the enzymatic
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