475941
Myokinase, Yeast
Szinonimák:
Myokinase, Yeast, Adenylate Kinase, ATP:AMP Phosphotransferase
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
CAS-szám:
MDL-szám:
UNSPSC kód:
12352202
NACRES:
NA.54
Javasolt termékek
Forma
lyophilized
Minőségi szint
specifikus aktivitás
≥10 units/mg solid
≥200 U/mg
gyártó/kereskedő neve
Calbiochem®
tárolási körülmény
OK to freeze
desiccated (hygroscopic)
pI
5.7
oldhatóság
water: 1 mg/mL
idegen aktivitás
ATPase ≤0.01%
Phosphoglycerate kinase ≤0.1%
kiszállítva
wet ice
tárolási hőmérséklet
−20°C
Általános leírás
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.
Figyelmeztetés
Toxicity: Standard Handling (A)
Egység definíció
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.
Fizikai forma
Lyophilized from potassium phosphate buffer.
Feloldás
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Egyéb megjegyzések
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.
Jogi információk
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Tárolási osztály kódja
13 - Non Combustible Solids
WGK
WGK 3
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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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
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
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
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
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