5′-Nucleotidase in Rat Liver Lysosomal Membranes is anchored via Glycosyl-Phosphatidylinositol

Yoshitaka Tanaka, Masaru Himeno, Ryo Taguchi, Hiroh Ikezawa, Keitaro Kato

研究成果: ジャーナルへの寄稿記事

3 引用 (Scopus)

抄録

We have previously demonstrated that 5′-nucleotidase, known as a plasma membrane enzyme, is also distributed both in rat liver tritosomal membranes and contents (J. Biochem. 101, 1077-1085, 1987). When the lysosomal membranes isolated from rat livers were incubated with phosphatidylinositol-specific phospholipase C purified from B. thuringiensis, about 70% of 5′-nucleotidase activity was released from the membranes. Judging from the result by phase separation with Triton X-114, the enzyme solubilized by the phospholipase C digestion showed a hydrophilic nature such as that of the tritosomal contents. Immunoblot analysis showed that the molecular weight of 5′-nucleotidase released from the lysosomal membranes by the phospholipase C digestion was almost identical with that of the enzymes from the Tritosomal contents. The above results showed that the phosphatidylinositol-specific phospholipase C-like enzyme in the lysosomes may be responsible for the conversion of the lysosomal membrane-bound 5′-nucleotidase to the soluble form present in the lysosomal matrix.

元の言語英語
ページ(範囲)597-603
ページ数7
ジャーナルCell structure and function
14
発行部数5
DOI
出版物ステータス出版済み - 1 1 1989

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Glycosylphosphatidylinositols
5'-Nucleotidase
Membranes
Liver
Phosphoinositide Phospholipase C
Type C Phospholipases
Enzymes
Digestion
Lysosomes
Molecular Weight
Cell Membrane

All Science Journal Classification (ASJC) codes

  • Physiology
  • Molecular Biology
  • Cell Biology

これを引用

5′-Nucleotidase in Rat Liver Lysosomal Membranes is anchored via Glycosyl-Phosphatidylinositol. / Tanaka, Yoshitaka; Himeno, Masaru; Taguchi, Ryo; Ikezawa, Hiroh; Kato, Keitaro.

:: Cell structure and function, 巻 14, 番号 5, 01.01.1989, p. 597-603.

研究成果: ジャーナルへの寄稿記事

Tanaka, Yoshitaka ; Himeno, Masaru ; Taguchi, Ryo ; Ikezawa, Hiroh ; Kato, Keitaro. / 5′-Nucleotidase in Rat Liver Lysosomal Membranes is anchored via Glycosyl-Phosphatidylinositol. :: Cell structure and function. 1989 ; 巻 14, 番号 5. pp. 597-603.
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abstract = "We have previously demonstrated that 5′-nucleotidase, known as a plasma membrane enzyme, is also distributed both in rat liver tritosomal membranes and contents (J. Biochem. 101, 1077-1085, 1987). When the lysosomal membranes isolated from rat livers were incubated with phosphatidylinositol-specific phospholipase C purified from B. thuringiensis, about 70{\%} of 5′-nucleotidase activity was released from the membranes. Judging from the result by phase separation with Triton X-114, the enzyme solubilized by the phospholipase C digestion showed a hydrophilic nature such as that of the tritosomal contents. Immunoblot analysis showed that the molecular weight of 5′-nucleotidase released from the lysosomal membranes by the phospholipase C digestion was almost identical with that of the enzymes from the Tritosomal contents. The above results showed that the phosphatidylinositol-specific phospholipase C-like enzyme in the lysosomes may be responsible for the conversion of the lysosomal membrane-bound 5′-nucleotidase to the soluble form present in the lysosomal matrix.",
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AU - Kato, Keitaro

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N2 - We have previously demonstrated that 5′-nucleotidase, known as a plasma membrane enzyme, is also distributed both in rat liver tritosomal membranes and contents (J. Biochem. 101, 1077-1085, 1987). When the lysosomal membranes isolated from rat livers were incubated with phosphatidylinositol-specific phospholipase C purified from B. thuringiensis, about 70% of 5′-nucleotidase activity was released from the membranes. Judging from the result by phase separation with Triton X-114, the enzyme solubilized by the phospholipase C digestion showed a hydrophilic nature such as that of the tritosomal contents. Immunoblot analysis showed that the molecular weight of 5′-nucleotidase released from the lysosomal membranes by the phospholipase C digestion was almost identical with that of the enzymes from the Tritosomal contents. The above results showed that the phosphatidylinositol-specific phospholipase C-like enzyme in the lysosomes may be responsible for the conversion of the lysosomal membrane-bound 5′-nucleotidase to the soluble form present in the lysosomal matrix.

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