Jauhiainen A, Vanha-Perttula T
Int J Biochem. 1987;19(3):267-74. doi: 10.1016/0020-711x(87)90030-9.
Acid and neutral alpha-mannosidase activities were studied in the bull reproductive tissues, isolated spermatozoa, epididymal and seminal vesicle secretion and seminal plasma. The acid enzyme in the seminal plasma mainly derived from the epididymal secretion, while the neutral one was enriched in the sperm cells. The latter activity in the seminal plasma appears to be due to an enzyme released from the cytoplasmic droplets in the epididymis. The acid enzyme had a molecular weight of 220,000-320,000, pI 7.3-6.0 and an optimum at pH 4.0. It was sensitive to swainsonine but was stimulated by Zn2+. The neutral enzyme had a molecular weight of 360,000-460,000, pI 5.4-4.7 and showed double optima at pH 5.5 and 6.0-7.0. It was resistant to swainsonine but was markedly activated by Co2+ or Fe2+. The neutral enzyme was also more sensitive to thermal inactivation than the acid one.
对公牛生殖组织、分离出的精子、附睾和精囊分泌物以及精浆中的酸性和中性α-甘露糖苷酶活性进行了研究。精浆中的酸性酶主要来源于附睾分泌物，而中性酶在精子细胞中含量丰富。精浆中后者的活性似乎是由于附睾中细胞质滴释放的一种酶。酸性酶的分子量为220,000 - 320,000，等电点为7.3 - 6.0，最适pH值为4.0。它对苦马豆素敏感，但受Zn2 +刺激。中性酶的分子量为360,000 - 460,000，等电点为5.4 - 4.7，在pH 5.5和6.0 - 7.0时表现出双最优值。它对苦马豆素具有抗性，但被Co2 +或Fe2 +显著激活。中性酶对热失活也比酸性酶更敏感。
