Tu A T, Hendon R R
Comp Biochem Physiol B. 1983;76(2):377-83. doi: 10.1016/0305-0491(83)90086-x.
Hyaluronidase was isolated from the lizard (Heloderma horridum horridum) crude venom. The chemical properties were characterized and compared to the same enzyme from other sources. The enzyme was found to be a single polypeptide chain with a molecular weight of 63,000 daltons. It possesses an isoelectric point and pH optimum of 5.0, and was observed to be extremely temperature sensitive. The role of hyaluronidase as a spreading factor which serves to aid in the diffusion of toxins has been suspected for a long time; yet no experimental proof has been offered until now. It was shown that hyaluronidase promotes the spread of the hemorrhagic area in mice when injected with hemorrhagic toxin. Thus experimental evidence is supplied for the first time that the enzyme plays a role as a "spreading factor" in the toxic action of venom.
透明质酸酶是从蜥蜴（Heloderma horridum horridum）的粗毒液中分离出来的。对其化学性质进行了表征，并与其他来源的同一种酶进行了比较。发现该酶是一条单多肽链，分子量为63,000道尔顿。它的等电点和最适pH值为5.0，并且观察到对温度极其敏感。长期以来，人们一直怀疑透明质酸酶作为一种扩散因子有助于毒素的扩散；但直到现在还没有提供实验证据。结果表明，当注射出血毒素时，透明质酸酶会促进小鼠出血区域的扩散。因此，首次提供了实验证据，证明该酶在毒液的毒性作用中起“扩散因子”的作用。
