Roy A C, Ratnam S S
Department of Obstetrics and Gynaecology, National University of Singapore, National University Hospital.
Arch Androl. 1990;25(1):1-4. doi: 10.3109/01485019008987586.
Human spermatozoa were extracted with 1% Triton X-100 and analyzed for oxytocinase (E.C. 3.4.11.3) activity by means of two synthetic peptides. S-benzyl-L-cysteine-p-nitroanilide (BCN) and L-leucine-p-nitroanilide (LN), separately as substrates. The specific activity (mean +/- SD) of this proteolytic enzyme at Vmax in eight different extracts was 0.150 +/- 0.072 and 1.392 +/- 0.602 mIU/10(6) cells using BCN and LN, respectively. The enzyme showed optimal activity at pH 7.2 when BCN was the substrate, and at pH 7.4 with LN as the substrate. Spermatozoal oxytocinase activity may be involved directly or indirectly in the reproductive mechanisms leading to sperm acrosome reaction and fertilization.
用1% Triton X - 100提取人精子,并通过两种合成肽分析催产素酶(E.C. 3.4.11.3)活性。分别以S -苄基 - L -半胱氨酸 - 对硝基苯胺(BCN)和L -亮氨酸 - 对硝基苯胺(LN)作为底物。在八种不同提取物中,该蛋白水解酶在Vmax时的比活性(平均值±标准差),使用BCN时为0.150±0.072 mIU/10⁶细胞,使用LN时为1.392±0.602 mIU/10⁶细胞。当BCN为底物时,该酶在pH 7.2时表现出最佳活性;以LN为底物时,在pH 7.4时表现出最佳活性。精子催产素酶活性可能直接或间接参与导致精子顶体反应和受精的生殖机制。