Isolation and characterization of Physarum profilin.

Isolation and characterization of Physarum profilin. Research Abstract Details 

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Isolation and characterization of Physarum profilin. Abstract Text:

K Ozaki,H Sugino,T Hasegawa,S Takahashi,S Hatano,

A protein that functionally resembles mammalian and Acanthamoeba profilins, has been purified from Physarum plasmodia. Physarum profilin consists of a single polypeptide with a molecular weight of 11,000-13,000. It has an isoelectric point of 5.35-5.40 under denaturing conditions. The amino acid composition of this protein is similar to those of profilins isolated from other sources. Physarum profilin prolongs the process of actin polymerization in a concentration-dependent fashion. This effect is much stronger for Physarum G-actin than for muscle G-actin.

Isolation and characterization of Physarum profilin. Publishing Authors By Initials

K Ozaki,H Sugino,T Hasegawa,S Takahashi,S Hatano,

For similar proteins research abstracts see: proteins research

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Isolation and characterization of Physarum profilin. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 93

Page Numbers: 295-8

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 1983

Isolation and characterization of Physarum profilin. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Isolation and characterization of Physarum profilin. Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Isolation and characterization of Physarum profilin. Information

Substance Name: Proteins

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Country: JAPAN

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MEDLINETA: J Biochem

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