Jones R E, Plymate S R, Fariss B L
J Androl. 1985 Sep-Oct;6(5):265-70. doi: 10.1002/j.1939-4640.1985.tb00844.x.
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.
对人类精子进行了研究,以确定是否存在长链脂肪酸辅酶A连接酶(AMP)(酶编号6.2.1.3)。采用放射性配体微孔滤膜技术测定连接酶活性,该活性在精子或用曲拉通X-100提取的蛋白质组分中很容易检测到,但在精浆中不存在。该测定针对pH、蛋白质浓度和孵育时间进行了优化。活性依赖于棕榈酸、ATP、辅酶A和二价阳离子。精子连接酶与其他组织中鉴定的连接酶相似,具有共同的最适pH值(约8.0 - 8.4),并且在孵育介质中对镁的偏好高于锰。