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形狀
lyophilized
品質等級
比活性
≥10 units/mg solid
≥200 U/mg
製造商／商標名
Calbiochem®
儲存條件
OK to freeze
desiccated (hygroscopic)
pI
5.7
溶解度
water: 1 mg/mL
異物活動
ATPase ≤0.01%
Phosphoglycerate kinase ≤0.1%
運輸包裝
wet ice
儲存溫度
−20°C
一般說明
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.
警告
Toxicity: Standard Handling (A)
單位定義
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.
外觀
Lyophilized from potassium phosphate buffer.
重構
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
其他說明
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.
法律資訊
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
儲存類別代碼
13 - Non Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
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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