Bhatnagar S K, Chaudhry P S, Anand S R
J Reprod Fertil. 1979 May;56(1):133-9. doi: 10.1530/jrf.0.0560133.
The cyclic AMP-phosphodiesterase (EC 3.1.4.17) of buffalo spermatozoa is distributed in the head, mid-piece and tail fractions and has multiple forms, 70% of which is in the bound form. The bound enzyme was not solubilized by Triton X-100, lubrol or hyamine 2389. Kinetic measurements of the soluble enzyme showed two apparent Km values for low and high cAMP concentrations, i.e. 4.5 and 100 micro M with Vmax values of 0.25 and 2.0 nmol cAMP hydrolysed min-1 mg protein-1. The bound enzyme had an apparent Km of 66.6 microM with a Vmax of 0.75 nmol cAMP hydrolysed min-1 mg protein-1. The pH for optimum enzyme activity was 7.5 and Mg2+ was essential for the activity of the soluble and bound enzymes. Methylxanthines, ATP, ADP and ppi inhibited the soluble and bound enzymes, ATP being the most potent inhibitor.
水牛精子的环磷酸腺苷磷酸二酯酶(EC 3.1.4.17)分布于头部、中段和尾部组分中,且具有多种形式,其中70%为结合形式。结合型酶不能被曲拉通X-100、十二烷基聚氧乙烯醚或十六烷基三甲基氢氧化铵溶解。对可溶性酶的动力学测量显示,对于低和高浓度的环磷酸腺苷有两个表观Km值,即4.5和100 μM,Vmax值分别为0.25和2.0 nmol环磷酸腺苷水解·min⁻¹·mg蛋白⁻¹。结合型酶的表观Km为66.6 μM,Vmax为0.75 nmol环磷酸腺苷水解·min⁻¹·mg蛋白⁻¹。酶活性的最适pH为7.5,Mg²⁺对可溶性和结合型酶的活性均至关重要。甲基黄嘌呤、ATP、ADP和焦磷酸抑制可溶性和结合型酶,ATP是最有效的抑制剂。