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首页> 外文期刊>The protein journal >Amaranth Globulin Polypeptide Heterogeneity.
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Amaranth Globulin Polypeptide Heterogeneity.

机译：mar菜球蛋白多肽异质性。

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摘要

The polypeptides integrating amaranth globulin-p and 11S-globulin were characterized by two-dimensional electrophoresis, ion-exchange chromatography and RP-HPLC. All polypeptides exhibited charge and hydrophobic heterogeneity. Almost all acid (A, pI 5-7) and basic (B, pI 9-10) polypeptides were present in both globulins, and the same happened with the unprocessed M polypeptides with pI in the range of 7-7.5 which fits well with a sequence containing both the A and B polypeptides. There were other polypeptides only present in 11S-globulin, like some of 41 and 16 kDa, which might come from another precursor or be the products of a different processing of the propolypeptide. These results suggested that, although amaranth subunits from different subfamilies are interchangeable in different oligomers, some structural differences between them might affect the assembly of globulin molecules. Structural differences arising from this behavior could account for the different physicochemical properties of globulin molecules.
机译：通过二维电泳，离子交换色谱和RP-HPLC对integrating菜红球蛋白-p和11S-球蛋白进行整合。所有多肽均表现出电荷和疏水异质性。两种球蛋白中几乎都存在酸性（A，pI 5-7）和碱性（B，pI 9-10）多肽，未加工的M多肽也是如此，pI在7-7.5的范围内，非常适合同时包含A和B多肽的序列。还有其他仅存在于11S球蛋白中的多肽，例如41 kDa和16 kDa的多肽，它们可能来自另一种前体，或者是原多肽的不同加工产物。这些结果表明，尽管来自不同亚家族的a菜亚基在不同的低聚物中可互换，但它们之间的某些结构差异可能会影响球蛋白分子的组装。由这种行为引起的结构差异可以解释球蛋白分子的不同理化特性。

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