PHENYLALANINE HYDROXYLASE FROM HUMAN KIDNEY

PHENYLALANINE HYDROXYLASE FROM HUMAN KIDNEY
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DOI:
10.1159/000458915
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发表时间:
1975-01-01
期刊:
ENZYME
影响因子:
--
通讯作者:
PIRSON, WD
PIRSON, WD
中科院分区:
其他
文献类型:
--
作者:
AYLING, JE;HELFAND, GD;PIRSON, WD

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在这份报告中,苯丙氨酸羟化酶的存在和水平,在人肾皮质的建立。在15个手术切除的肾脏中发现的平均活性为47.2 ± 11.2 mU/g组织湿重。在相同的实验条件下测定的两个人肝活检组织的平均值为217 mU/g组织。5个尸检肝脏获得2.5-4小时死后,四个不含活性,只有1-2%的正常被发现在第五。尸检肾脏同样没有活性。在尸检肝匀浆中无法证明存在高活性降解酶;已确定缺乏活性不是由于抑制组分。一种可能的解释这种现象进行了讨论。根据其他地方发表的工作[3],肾脏和肝脏的酶似乎是相似的。因此,手术切除的肾脏提供了另一种来源的人苯丙氨酸羟化酶,可用于研究苯丙酮尿症。
In this report the presence,and level, of phenylalanine hydroxylase in the cortex of human kidney is established. The average activity found in 15 surgically removed kidneys was 47.2 ± 11.2 mU/g wet weight of tissue. The average value, determined under the same experimental conditions, for two human liver biopsies was 217 mU/g tissue. Of five autopsy livers obtained 2.5-4 h postmortem, four contained no activity,and only 1-2% of normal was found in the fifth. Autopsy kidneys were similarly inactive. The presence of a highly active degradative enzyme could not be demonstrated in autopsy liver homogenates; it was established that the lack of activity was not due to an inhibitory component. A possible interpretation of this phenomenon is discussed. According to work published elsewhere [3] the kidney and liver enzymes appear to be similar. Thus, surgically removed kidneys provide an alternative source of human phenylalanine hydroxylase which can be used to study phenylketonuria.