Year: 1985
Type: article
Abstract: 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.
Source: Journal of Andrology
Authors: ROBERT E. JONES, STEPHEN R. PLYMATE, BRUCE L. FARISS
Institution: Madigan Army Medical Center
Language: English
Subfield: Reproductive Medicine
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
OpenAlex ID: W1521712052