Changes of aspartate aminotransferase and alanine aminotransferase activity in vitamin B6 deficient rat.
Takashi Ueda, Masaaki Arakawa, Yahito KOTAKE
Abstract
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Takashi Ueda, Masaaki Arakawa, Yahito KOTAKE
Abstract
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The aspartate aminotransferase and alanine aminotransferase activities in vitamin B6 deficient rats were assayed, The activities of aspartate aminotransferase and alanine aminotransferase were reduced in the supernatant fraction, while their activities were preserved in the mitochondrial fraction. With the addition of pyridoxal phosphate in vitro to the liver or kidney of vitamin B6 deficient rats, the supernatant aspartate aminotransferase recovered its activity to a respectable degree, while alanine aminotransferase not so much. The addition of pyridoxal phosphate in vitro had no influence upon tbe activity of mitochondrial aspartate aminotransferase and alanine aminotransferase. The results of these experiments indicate that these supernatant transaminases are affected by the diminution of vitamin B6 content.
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The aspartate aminotransferase and alanine aminotransferase activities in vitamin B6 deficient rats were assayed, The activities of aspartate aminotransferase and alanine aminotransferase were reduced in the supernatant fraction, while their activities were preserved in the mitochondrial fraction. With the addition of pyridoxal phosphate in vitro to the liver or kidney of vitamin B6 deficient rats, the supernatant aspartate aminotransferase recovered its activity to a respectable degree, while alanine aminotransferase not so much. The addition of pyridoxal phosphate in vitro had no influence upon tbe activity of mitochondrial aspartate aminotransferase and alanine aminotransferase. The results of these experiments indicate that these supernatant transaminases are affected by the diminution of vitamin B6 content.
Key concepts: Alanine, Pyridoxal, Pyridoxal phosphate, Vitamin b6, Alanine aminotransferase, Pyridoxine, In vitro, Chemistry