Baker N J, Gandhi S S
Arch Virol. 1976;52(1-2):7-18. doi: 10.1007/BF01317860.
The neuraminidases of different strains of influenza virus varied in their stability at 37 degrees C. The enzymes of the strains with N1 neuraminidases were found to be unstable during incubation at 37 degrees C whereas the enzymes of the strains with the N2 neuraminidases were stable. Among the strains with N2 neuraminidases, the enzymes of some strains were inactivated during dialysis at 37 degrees C whereas the enzymes of others were stable. This observed loss of enzyme activity during dialysis at 37 degrees C was not restricted to a single substrate as the same loss of enzyme activity was observed irrespective of the size of the substrate used in the assay. The enzymically inactive neuraminidase was found to be non-antigenic and non-immunogenic. The inactivation of the enzyme could be prevented by the addition of Ca++ but not Mg++. Out results suggest that Ca++ is essential for the stability of the enzyme at 37 degrees C. The results would also suggest that the enzymic, antigenic and immunogenic sites are either the same or very closely situated on the surface of the neuraminidase molecule.
不同株流感病毒的神经氨酸酶在37℃时的稳定性各不相同。发现具有N1神经氨酸酶的毒株的酶在37℃孵育期间不稳定,而具有N2神经氨酸酶的毒株的酶则稳定。在具有N2神经氨酸酶的毒株中,一些毒株的酶在37℃透析期间失活,而其他毒株的酶则稳定。在37℃透析期间观察到的这种酶活性丧失并不局限于单一底物,因为无论测定中使用的底物大小如何,都观察到相同的酶活性丧失。发现无酶活性的神经氨酸酶无抗原性且无免疫原性。添加Ca++可防止酶失活,但添加Mg++则不能。我们的结果表明,Ca++对于酶在37℃时的稳定性至关重要。结果还表明,酶活性位点、抗原位点和免疫原性位点要么相同,要么在神经氨酸酶分子表面非常靠近。