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The NH2‐terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are Nα‐acetylated
[摘要]

Rat liver proteasome (multicatalytic proteinase complex) is a 20S-ring shaped particle having a molecular mass of 750 kDa, and iscomposed of at least 13 non-identical components ranging from 21 to 31 kDa in size. We found here that the NH2-terminal residues of all the known 13 components, except for C5, are not reactive to phenylisothiocyanate. Among them, components C2, C3 and C8 are blocked in their NH2-termini with Nα-acetyl-Met, Nα-acetyl-Ala, and Nα-acetyl-Ser, respectively. The NH2-terminal portions of C2, C3, and C8 exhibit sequence similarity to one another, but that of the non-blocked component C5 differs from those of C2, C3, and C8.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[关键词] Nα-acetylation;Proteasome;Multicatalytic proteinase;FAB;fast atom bombrdment;HPLC;high performance liquid chromatography [时效性] 
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