Branched-chain amino acid aminotransferase in mouse testicular tissue

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Authors:
E. E. Montamat
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,
J. Moreno
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, and
A. Blanco
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DOI:
https://doi.org/10.1530/jrf.0.0530117
Volume/Issue:
Volume 53: Issue 1
Page Range:
117–123
Article Type:
Research Article
Online Publication Date:
May 1978
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Summary. Branched-chain amino acid aminotransferase (l-leucine:2-oxoglutarate aminotransferase, EC 2.6.1.6) activity was determined in several tissues of the mouse. Testis homogenates presented a specific activity very close to that of heart extracts which were the most active. Enzyme activity was detectable in testes from 5-day-old mice and increased steadily during development to reach a maximum at the 20th day of life. The transaminase was present in the cytosol of testicular homogenates and also associated, probably in the matrix, with a special type of mitochondria present in spermatozoa and gametogenic cells. The enzyme from testis is active against the three branched-chain amino acids and catalyses the reaction in both directions. Highest activity and lowest Km were obtained with l-leucine. Activity with l-valine was the lowest. The enzyme from the mitochondrial fraction showed identical properties to that from the soluble phase. The possible participation of this aminotransferase in a shuttle system transferring reducing equivalents from cytoplasm to mitochondria is postulated.

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Print ISSN:
1470-1626
Online ISSN:
1741-7899