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首页> 外文OA文献 >Evolution of phosphagen kinase. Isolation, characterization and cDNA-derived amino acid sequence of two-domain arginine kinase from the sea anemone Anthopleura japonicus.
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Evolution of phosphagen kinase. Isolation, characterization and cDNA-derived amino acid sequence of two-domain arginine kinase from the sea anemone Anthopleura japonicus.

机译：磷酸激酶的进化。海葵Anthopleura japonicus的两个结构域精氨酸激酶的分离，鉴定和cDNA氨基酸序列。

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摘要

Arginine kinase (AK) was isolated from the body wall muscle of the primitive sea anemone Anthopleura japonicus by Ultrogel AcA34 gel filtration, DEAE-32 chromatography and elution on a Cosmogel-SP column. The denatured molecular mass as determined with SDS/PAGE was 80 kDa, twice that of the usual AK subunit, indicating that this AK has an unusual two-domain structure. The native form was eluted on a Superose 12 column with the same retention time as that of rabbit homodimeric creatine kinase, indicating that Anthopleura AK is a monomer of 80 kDa. The isolated enzyme gave a specific activity of 100-120 micromol of Pi/min per mg of protein in the pH range 7.9-9.1 for the forward reaction. The enzyme is fully activated by Ca2+, as it is with Mg2+. The cDNA-derived amino acid sequence of 715 residues of Anthopleura AK was determined. The validity of the sequence was supported by chemical sequencing of internal tryptic peptides. A bridge intron of 686 bp, which separates the two domains of Anthopleura AK, is present between the second and third nucleotide in the codon of Ala-364. This is the first two-domain AK to be sequenced. Anthopleura AK shows 48-54% amino acid sequence identity with known invertebrate AKs, and also shows a lower, but significant, similarity (39-46%) to marine worm glycocyamine kinase and rabbit creatine kinase.
机译：通过Ultrogel AcA34凝胶过滤，DEAE-32色谱和在Cosmogel-SP柱上洗脱，从原始海葵Anthopleura japonicus的体壁肌肉中分离出精氨酸激酶（AK）。用SDS / PAGE测定的变性分子量为80kDa，是通常的AK亚单位的两倍，表明该AK具有不寻常的两结构域结构。天然形式在Superose 12色谱柱上洗脱，保留时间与兔同型二聚肌酸激酶相同，表明Anthopleura AK是80 kDa的单体。在正向反应的pH范围为7.9-9.1的情况下，分离出的酶的特异活性为每mg蛋白质100-120 micromol Pi / min。与Mg2 +一样，该酶被Ca2 +完全激活。确定了Anthopleura AK的715个残基的cDNA氨基酸序列。内部胰蛋白酶肽的化学测序支持了该序列的有效性。 Ala-364密码子的第二个和第三个核苷酸之间存在一个686 bp的桥内含子，它分隔了Anthopleura AK的两个结构域。这是要排序的第一个两域AK。 Anplepleura AK与已知的无脊椎动物AKs显示48-54％的氨基酸序列同一性，并且与海洋蠕虫糖胺激酶和兔肌酸激酶的相似性较低（39-46％）。

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