Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b 5 reductase by HPLC mapping

Minoru Tamura, Toshitsugu Yubisui, Masazumi Takeshita, Shun-Ichiro Kawabata, Toshiyuki Miyata, Sadaaki Iwanaga

研究成果: ジャーナルへの寄稿記事

11 引用 (Scopus)

抄録

NADH-cytochrome b 5 reductases purified from bovine erythrocytes and from bovine brain and liver microsomes solubilized with lysosomal protease were subjected to structural analysis by using HPLC mapping, amino acid analysis of the resulting peptides, and NH 2 -terminal sequence analysis of apoproteins. HPLC maps of the tryptic peptides derived from these enzymes were very similar to each other, and amino acid analysis of the HPLC-separated peptides indicated that the structures of these enzymes are identical except for the NH 2 -terminal region. The NH 2 -terminal sequence of the brain enzyme determined by automated Edman degradation was as follows:NH 2 -Phe-Gln-Arg-Ser-Thr-Pro-Ala-Ile-Thr-Leu-Glu-Asn-Pro-Asp-Ile-Lys-Tyr-Pro-Leu-Arg-Leu-Ile-Asp-Lys-Glu-Val-Ile-This sequence is identical to that of liver enzyme except that the liver enzyme started at the 3rd Arg or 4th Ser. The NH 2 -terminal amino acid residue of the soluble erythrocyte enzyme was not detected by automated Edman degradation. The sequence analysis of a tryptic peptide from the erythrocyte enzyme indicated that Leu is present before the NH 2 -terminal Phe of the brain enzyme. The recently reported sequence of the apparently identical protein (Ozols et al. (1985) J. Biol. Chem. 260, 11953-11961) differs in two amino acid assignments from our sequence.

元の言語英語
ページ(範囲)1147-1159
ページ数13
ジャーナルJournal of biochemistry
101
発行部数5
DOI
出版物ステータス出版済み - 1 1 1987

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Cytochromes b5
Liver
NAD
Brain
Oxidoreductases
Erythrocytes
High Pressure Liquid Chromatography
Enzymes
Amino Acids
Peptides
Sequence Analysis
Degradation
Apoproteins
Liver Microsomes
Structural analysis
Peptide Hydrolases

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

これを引用

Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b 5 reductase by HPLC mapping . / Tamura, Minoru; Yubisui, Toshitsugu; Takeshita, Masazumi; Kawabata, Shun-Ichiro; Miyata, Toshiyuki; Iwanaga, Sadaaki.

:: Journal of biochemistry, 巻 101, 番号 5, 01.01.1987, p. 1147-1159.

研究成果: ジャーナルへの寄稿記事

Tamura, Minoru ; Yubisui, Toshitsugu ; Takeshita, Masazumi ; Kawabata, Shun-Ichiro ; Miyata, Toshiyuki ; Iwanaga, Sadaaki. / Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b 5 reductase by HPLC mapping :: Journal of biochemistry. 1987 ; 巻 101, 番号 5. pp. 1147-1159.
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abstract = "NADH-cytochrome b 5 reductases purified from bovine erythrocytes and from bovine brain and liver microsomes solubilized with lysosomal protease were subjected to structural analysis by using HPLC mapping, amino acid analysis of the resulting peptides, and NH 2 -terminal sequence analysis of apoproteins. HPLC maps of the tryptic peptides derived from these enzymes were very similar to each other, and amino acid analysis of the HPLC-separated peptides indicated that the structures of these enzymes are identical except for the NH 2 -terminal region. The NH 2 -terminal sequence of the brain enzyme determined by automated Edman degradation was as follows:NH 2 -Phe-Gln-Arg-Ser-Thr-Pro-Ala-Ile-Thr-Leu-Glu-Asn-Pro-Asp-Ile-Lys-Tyr-Pro-Leu-Arg-Leu-Ile-Asp-Lys-Glu-Val-Ile-This sequence is identical to that of liver enzyme except that the liver enzyme started at the 3rd Arg or 4th Ser. The NH 2 -terminal amino acid residue of the soluble erythrocyte enzyme was not detected by automated Edman degradation. The sequence analysis of a tryptic peptide from the erythrocyte enzyme indicated that Leu is present before the NH 2 -terminal Phe of the brain enzyme. The recently reported sequence of the apparently identical protein (Ozols et al. (1985) J. Biol. Chem. 260, 11953-11961) differs in two amino acid assignments from our sequence.",
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