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Journal of Andrology, Vol 6, Issue 5 265-270, Copyright © 1985 by The American Society of Andrology

JOURNAL ARTICLE

Activation of palmitic acid by human spermatozoa

R. E. Jones, S. R. Plymate and B. L. Fariss

Human spermatozoa were studied to determine if a long chain fatty acid, CoASH ligase (AMP) (E.C. 6.2.1.3), was present. Ligase activity was measured with a radioligand millipore filter technique and was readily detectable in spermatozoa or in the protein fraction extracted with Triton X-100, but was not present in seminal plasma. The assay was optimized for pH, protein concentration, and incubation time. Activity was dependent upon palmitic acid, ATP, coenzyme A, and a divalent cation. Sperm ligase appeared similar to the ligase characterized from other tissues by sharing a common pH optimum (approximately 8.0-8.4), and a preference for magnesium over manganese in the incubation media.




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Copyright © 1985 by The American Society of Andrology.