PROTEIN-PROTEIN INTERACTIONS OF PROTEOLYTIC FRAGMENTS OF ACTIN

被引：27
作者：
JOHNSON, P
WESTER, PJ
HIKIDA, RS
机构：
[1] OHIO UNIV, COLL OSTEOPATH MED, ATHENS, OH 45701 USA
[2] OHIO UNIV, DEPT ZOOL & MICROBIOL, ATHENS, OH 45701 USA
来源：
BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 578卷 / 01期
关键词：
Actin; Myosin; Protein-protein interaction; Proteolytic fragmentation; Tropomyosin;
D O I：
10.1016/0005-2795(79)90133-8
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：
Proteolytic fragments of actin, prepared by removal of up to sixty-eight residues from the N-terminal end of the molecule, can form filamentous structures after denaturation in urea solution. The filaments have a diameter similar to F-actin filaments and interact with myosin and tropomyosin. A fragment comprising residues 1 to 207 of the actin sequence did not form filaments or interact with myosin after the urea treatment. © 1979.
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页码：253 / 257
页数：5
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