人唾液和胰腺α-淀粉酶同工酶的分离与鉴定
Isolation and characterization of isoenzymes of human salivary and pancreatic alpha-amylase.
作者信息
Rosenmund H, Kaczmarek M J
出版信息
Clin Chim Acta. 1976 Sep 6;71(2):185-9. doi: 10.1016/0009-8981(76)90529-5.
Human salivary and pancreatic alpha-amylase (1,4-glucan 4-glucanohydrolase, EC 3.2.1.1) were separated by electrofocusing. In the first case we obtained six isoenzymes with isoelectric points of pH 5.70, 5.72, 6.23, 6.32, 6.73 and 6.88. Human pancreatic alpha-amylase has been separated into eight isoenzymes with isoelectric points of pH 5.72, 5.77, 5.88, 6.05, 6.23, 6.69, 6.72 and 6.95. Some of the isoenzymes were shown to be sialoproteins; others representing about 80% of the total activity did not contain neuraminic acid. The molecular weight of the non-sialoproteinic isoenzymes was found to be about 47 000 in all cases.
通过电聚焦法分离了人唾液和胰腺α-淀粉酶（1,4-葡聚糖4-葡聚糖水解酶，EC 3.2.1.1）。在第一种情况下，我们获得了六种同工酶，其等电点分别为pH 5.70、5.72、6.23、6.32、6.73和6.88。人胰腺α-淀粉酶已被分离为八种同工酶，其等电点分别为pH 5.72、5.77、5.88、6.05、6.23、6.69、6.72和6.95。一些同工酶被证明是唾液酸蛋白；其他占总活性约80%的同工酶不含神经氨酸。在所有情况下，非唾液酸蛋白同工酶的分子量约为47000。
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