Isolation of beta-N-acetylhexosaminidase from rabbit semen and its role in fertilization.
Isolation of beta-N-acetylhexosaminidase from rabbit semen and its role in fertilization.
复制标题
从兔精液中分离β-N-乙酰己糖胺酶及其在受精中的作用。
DOI:
10.1042/bj1910827
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发表时间:
1980
期刊:
影响因子:
--
通讯作者:
Srivastava,PN
中科院分区:
文献类型:
--
作者:
Farooqui,AA;Srivastava,PN
Beta-N-Acetylhexosaminidase was purified from the rabbit seminal plasma by a three-step procedure involving hydroxyapatite, Sephadex G-200 and concanavalin A–Sepharose chromatography. The specific activity of the purified preparation was 56mu mol/min per mg of protein, which represented a 226-fold purification and a 54% yield of the enzyme activity. The purified enzyme was electrophoretically homogeneous. The homogeneous enzyme showed optimal activity at pH4.0. The apparent Km value and Vmax. were 1.4 mM and 56mu mol/min per mg of protein respectively. Metal ions such as Ag + and Hg2+ and p-chloromercuribenzoate strongly inhibited the enzyme activity. The treatment of rabbit ova with a mixture of Beta-N-acetylhexosaminidase and arylsulphatase A results in the swelling of the zona pellucida.