The evolution of peroxisomal and mitochondrial alanine: Glyoxylate aminotransferase 1 in mammalian liver

Yoshikazu Takada; Tomoo Noguchi

doi:10.1016/0006-291X(82)91844-7

The evolution of peroxisomal and mitochondrial alanine: Glyoxylate aminotransferase 1 in mammalian liver

Yoshikazu Takada
, Tomoo Noguchi

研究成果: 雜誌貢獻 › 文章 › 同行評審

12 引文斯高帕斯（Scopus）

摘要

Immunological distances of alanine: glyoxylate aminotransferase 1 (serine:pyruvate aminotransferase) in mitochondria or peroxisomes from eight different mammalian liver were determined with rabbit anti-serum against the mitochondrial enzyme of rat liver by microcomplement fixation. Results suggest that heterotopic alanine:glyoxylate aminotransferase 1 are orthologous proteins and their subcellular localization and substrate specificity changed during rapid molecular evolution.

原文	英語
頁（從 - 到）	153-157
頁數	5
期刊	Biochemical and Biophysical Research Communications
卷	108
發行號	1
DOIs	https://doi.org/10.1016/0006-291X(82)91844-7
出版狀態	已發佈 - 9月 16 1982
對外發佈	是

ASJC Scopus subject areas

分子生物學
生物物理學
生物化學
細胞生物學

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10.1016/0006-291X(82)91844-7

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abstract = "Immunological distances of alanine: glyoxylate aminotransferase 1 (serine:pyruvate aminotransferase) in mitochondria or peroxisomes from eight different mammalian liver were determined with rabbit anti-serum against the mitochondrial enzyme of rat liver by microcomplement fixation. Results suggest that heterotopic alanine:glyoxylate aminotransferase 1 are orthologous proteins and their subcellular localization and substrate specificity changed during rapid molecular evolution.",

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AU - Noguchi, Tomoo

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The evolution of peroxisomal and mitochondrial alanine: Glyoxylate aminotransferase 1 in mammalian liver

摘要

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