ACTIN IN MAMMALIAN LENS

被引：70

作者：

KIBBELAAR, MA ^{[1
]}

SELTENVERSTEEGEN, AME ^{[1
]}

DUNIA, I ^{[1
]}

BENEDETTI, EL ^{[1
]}

BLOEMENDAL, H ^{[1
]}

机构：

[1] UNIV PARIS 7,CNRS,INST RECH BIOL MOLEC,F-75221 PARIS 05,FRANCE

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1979年 / 95卷 / 03期

关键词：

D O I：

10.1111/j.1432-1033.1979.tb12995.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In this paper evidence is provided that one of the protein components of the water‐soluble fraction of the calf lens binds specifically to deoxyribonuclease I (DNAse I). On the basis of this property, the polypeptide could be purified by applying DNAse I affinity chromatography. Concomitantly a protein of Mr 55000 and a rather large amount of α‐crystallin copurify with this polypeptide, which has a molecular weight of 42000. Highly purified 42000‐Mr protein was also obtained by extraction of the water‐insoluble fraction of the calf lens with 2‐{[tris(hydroxymethyl)methyl]amino}ethanesulfonic acid followed by gel filtration. Amino acid analyses, peptide mapping and electron microscopy show that the protein obtained from both lens fractions is identical to non‐muscle actin. Furthermore the amino acid composition of the 55000‐Mr protein is identical to hog stomach skeletin and very similar to calf brain desmin. Copyright © 1979, Wiley Blackwell. All rights reserved

引用

页码：543 / 549

页数：7

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