酵母氨肽酶I的四级结构。1. 分子形式和亚基大小。
The quaternary structure of yeast aminopeptidase I. 1. Molecular forms and subunit size.
作者信息
Metz G, Marx R, Röhm K H
出版信息
Z Naturforsch C Biosci. 1977 Nov-Dec;32(11-12):929-37. doi: 10.1515/znc-1977-11-1209.
The smallest active form of aminopeptidase I (EC 3.4.11.1) from yeast has a molecular weight of 6.4 X 10(5). At neutral pH the active enzyme is in equilibrium with two inactive subfragments (Mr = 3.2 X 10(5) and 1.1 X 10(5)) as well as with higher aggregates (Mr greater than or equal 1.2 X 10(6)). All of these species may be dissociated to give a single type of subunits with a molecular weight of 5.3 X 10(4). It is concluded that the active enzyme is a dodecamer whereas the subfragments correspond to dimeric and hexameric forms.
来自酵母的氨肽酶I（EC 3.4.11.1）的最小活性形式分子量为6.4×10⁵。在中性pH条件下，活性酶与两个无活性的亚片段（Mr = 3.2×10⁵和1.1×10⁵）以及更高聚集体（Mr≥1.2×10⁶）处于平衡状态。所有这些物种都可以解离成单一类型的亚基，分子量为5.3×10⁴。得出的结论是，活性酶是一个十二聚体，而亚片段对应于二聚体和六聚体形式。
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