Spontaneous and tryptic degradation of virus particles and structural components of adenoviruses.

Spontaneous and tryptic degradation of virus particles and structural components of adenoviruses.
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病毒颗粒和腺病毒结构成分的自发和胰蛋白酶降解。

DOI:
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发表时间:
1971
影响因子:
3.8
通讯作者:
J. Skehel
J. Skehel
中科院分区:
医学3区
文献类型:
--
作者:
H. Pereira;J. Skehel

文献摘要

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摘要 对腺病毒多肽组分的电泳分析表明,无论是纯化的病毒制剂还是分离的抗原,在储存过程中六邻体和五元碱基都被降解。这两个蛋白质组分也被胰酶降解,并对天然六角体的胰酶消化产物进行了详细的检测。结果表明,它们由6种多肽组成,可能是六邻体多肽上三个不同位置的胰酶作用的结果。 自发降解和胰酶降解的六邻体和五元碱基蛋白都保留了它们的形态和抗原特性。
Summary Electrophoretic analyses of the polypeptide components of adenovirus indicate that both the hexon and the penton base are degraded during storage of either purified virus preparations or isolated antigens. These two protein components are also degraded by trypsin and the products of tryptic digestion of native hexons were examined in detail. They were shown to consist of six polypeptide species which may result from tryptic action at three distinct sites on the hexon polypeptide. Both spontaneously degraded and trypsinized hexon and penton base proteins retained their morphological and antigenic characteristics.