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lyophilized
品質水準
比活性
≥10 units/mg solid
≥200 U/mg
メーカー／製品名
Calbiochem®
保管条件
OK to freeze
desiccated (hygroscopic)
pI
5.7
溶解性
water: 1 mg/mL
その他の活性
ATPase ≤0.01%
Phosphoglycerate kinase ≤0.1%
輸送温度
wet ice
保管温度
−20°C
詳細
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)
単位の定義
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.
物理的形状
Lyophilized from potassium phosphate buffer.
再構成
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
その他情報
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.
法的情報
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
保管分類コード
13 - Non Combustible Solids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
475941-1KU:
試験成績書（COA）
製品のロット番号・バッチ番号を入力して、試験成績書（COA） を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。
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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