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蚯蚓血红蛋白一条主要多肽链的氨基酸序列。

The amino acid sequence of a major polypeptide chain of earthworm hemoglobin.

作者信息

Garlick R L, Riggs A F

出版信息

J Biol Chem. 1982 Aug 10;257(15):9005-15.

PMID:7096348
Abstract

The amino acid sequence has been determined for polypeptide chain AIII of the major component of the hemoglobin (erythrocruorin) from the earthworm, Lumbricus terrestris. The chain has 157 residues and a molecular weight of 17,496. Although the extent of sequence identity with other globin chains is only 17-18%, analysis of the sequence leads to the conclusion that the secondary structure of the chain is very similar to those of vertebrate globins and that about 60-70% of the amino acid residues are in alpha helices. The D helix appears to be missing, as it is from the alpha chain of human hemoglobin and from the monomeric hemoglobin of Glycera dibranchiata, another annelid worm. This is the first sequence obtained from one of the "giant" extracellular hemoglobins of invertebrate animals.

摘要

已确定来自蚯蚓(陆正蚓)的血红蛋白(蚯蚓血红蛋白)主要成分的多肽链AIII的氨基酸序列。该链有157个残基,分子量为17496。尽管与其他球蛋白链的序列同一性程度仅为17 - 18%,但对该序列的分析得出结论,该链的二级结构与脊椎动物球蛋白的二级结构非常相似,约60 - 70%的氨基酸残基处于α螺旋中。D螺旋似乎缺失,就像在人类血红蛋白的α链以及另一种环节动物双鳃甘油虫的单体血红蛋白中一样。这是从无脊椎动物的“巨型”细胞外血红蛋白之一获得的首个序列。

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