Complementary DNA sequence for a 42 kDa rat kidney choline/ethanolamine kinase

C. Aoyama, Kinichi Nakashima, M. Matsui, K. Ishidate

研究成果: ジャーナルへの寄稿記事

28 引用 (Scopus)

抄録

By means of peptide sequence information, several cDNA clones encoding a 42 kDa choline/ethanolamine kinase were isolated from a rat kidney cDNA library. Eight clones were sequenced with all of them resulting in identical overlapping nucleotide sequences. Four of them possessed entire open reading frame which could encode 394 amino acids with a calculated molecular size of 45,100. The predicted amino acid sequence contained all of the internal peptide fragment sequences derived from the purified 42 kDa enzyme. When the open reading frame was introduced into pGEX-2T vector and transfected into E. coli cells, a significant choline/ethanolamine kinase activity did appear in the cell lysate. A homology comparison with the previously reported choline kinase cDNAs (CKR1 and CKR2) from rat liver showed 66%-68% in entire nucleotide sequences and 57%-59% in amino acid sequences, indicating that the cloned cDNA here must be a novel CK/EK gene product.

元の言語英語
ページ(範囲)1-7
ページ数7
ジャーナルBiochimica et Biophysica Acta - Lipids and Lipid Metabolism
1390
発行部数1
DOI
出版物ステータス出版済み - 2 5 1998
外部発表Yes

Fingerprint

Choline Kinase
DNA sequences
Choline
Rats
Complementary DNA
Kidney
Amino Acids
Open Reading Frames
Amino Acid Sequence
Nucleotides
Clone Cells
Peptide Fragments
Gene Library
Liver
Escherichia coli
Genes
Peptides
Enzymes
ethanolamine kinase

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Endocrinology

これを引用

Complementary DNA sequence for a 42 kDa rat kidney choline/ethanolamine kinase. / Aoyama, C.; Nakashima, Kinichi; Matsui, M.; Ishidate, K.

:: Biochimica et Biophysica Acta - Lipids and Lipid Metabolism, 巻 1390, 番号 1, 05.02.1998, p. 1-7.

研究成果: ジャーナルへの寄稿記事

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abstract = "By means of peptide sequence information, several cDNA clones encoding a 42 kDa choline/ethanolamine kinase were isolated from a rat kidney cDNA library. Eight clones were sequenced with all of them resulting in identical overlapping nucleotide sequences. Four of them possessed entire open reading frame which could encode 394 amino acids with a calculated molecular size of 45,100. The predicted amino acid sequence contained all of the internal peptide fragment sequences derived from the purified 42 kDa enzyme. When the open reading frame was introduced into pGEX-2T vector and transfected into E. coli cells, a significant choline/ethanolamine kinase activity did appear in the cell lysate. A homology comparison with the previously reported choline kinase cDNAs (CKR1 and CKR2) from rat liver showed 66{\%}-68{\%} in entire nucleotide sequences and 57{\%}-59{\%} in amino acid sequences, indicating that the cloned cDNA here must be a novel CK/EK gene product.",
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