β-D-N-乙酰己糖胺酶的研究。正常受试者和桑德霍夫病患者组织中的各种同工酶。
Studies on beta-D-N-acetylhexosaminidase. Various isozymes in tissues of normal subjects and Sandhoff's disease patients.
作者信息
Srivastava S K, Wiktorowicz J, Klebe R, Awasthi Y C
出版信息
Biochim Biophys Acta. 1975 Aug 26;397(2):428-36. doi: 10.1016/0005-2744(75)90132-1.
Hexosaminidase (EC 3.2.1.51) activity from human liver and kidney extract was completely precipitated by anti-hexosaminidase A antiserum and 80 to 90% by anti-hexosaminidase B antiserum. Immunologically distinct hexosaminidase "C" could not be detected in these tissues. The final fractions of hexosaminidase A eluted from DE-52 chromatography were resolved into several enzymatically active components by rechromatography. Compared to hexosaminidase A and B, these minor components are more anodal in polyacrylamide disc electrophoresis. The residual activity of hexosaminidase from liver and fibroblasts of patients with Sandhoff's disease has also been resolved into similar components. The enzyme activity of these more anodal hexosaminidase components was precipitated completely by anti-hexosaminidase A anti-serum and partially by anti-hexosaminidase B antiserum. The minor, more anodal components probably represent hexosaminidase molecules having an altered ratio of subunits or the degradation products of hexosaminidase A.
人肝脏和肾脏提取物中的己糖胺酶（EC 3.2.1.51）活性可被抗己糖胺酶A抗血清完全沉淀，被抗己糖胺酶B抗血清沉淀80%至90%。在这些组织中未检测到免疫上不同的己糖胺酶“C”。从DE - 52柱层析洗脱的己糖胺酶A的最终组分通过再层析被分离成几个具有酶活性的成分。与己糖胺酶A和B相比，这些次要成分在聚丙烯酰胺圆盘电泳中更偏向阳极。桑德霍夫病患者肝脏和成纤维细胞中己糖胺酶的残余活性也被分离成类似的成分。这些更偏向阳极的己糖胺酶成分的酶活性可被抗己糖胺酶A抗血清完全沉淀，被抗己糖胺酶B抗血清部分沉淀。这些次要的、更偏向阳极的成分可能代表亚基比例改变的己糖胺酶分子或己糖胺酶A的降解产物。
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