English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

A 45 K M, G-actin-binding protein was isolated from bovine aorta. This protein had an amino acid composition very similar to that of 84 K M, gelsolin and cross-reacted with anti-gelsolin antibodies. The 45 K M, protein consisted of two isoforms, I and II, as revealed by isoelectric focusing. Isoform I was slightly more acidic than isoform II and more abundant. Isoform II was not distinguishable from a chymotrypic peptide, CT47, of gelsolin in chain weight and isoelectric point values. The 45 K M, protein is shown to bind to G-actin by chemical cross-linking. It considerably lowered the initial rate of actin polymerization, but the inhibition became much less marked at a steady state, suggesting that the binding of this protein to actin was not so tight as CT47. Both isoforms of the 45 K M, protein were detected in a guanidine-HCl extract of freshly obtained bovine aorta. It is suggested that the 45 K M, protein derived from 84 K M, gelsolin exists in viva. A number of actin-binding proteins regulate dynamic state of actin filaments that are involved in cell motility and shape formation (for reviews, see l3, 14). In vertebrate smooth muscle (bovine aorta), Nonomura and his collaborators have isolated gelsolin-like 84 K M, protein that Ca“-dependently severs actin filaments (5). This protein called ‘actin length determinator’ has been shown to control the interactions between myosin and actin in the presence of ATP (4). During the course of preparing the 84 K M, protein from bovine aorta according to Ebisawa er al. (5), a 45 K M, actin-binding protein was isolated in the present study. However, this peptide turned out to be a proteolytic product of the 84 K M, protein. In view of the natural occurrence of this 45 K M, peptide 3T0 whom reprint request should be addressed in bovine aorta, its possible relationship to the mother protein is discussed in this article. MATERIALS AND METHODS

GELSOLIN-RELATED 45 K M, ACTIN-BINDING PROTEIN FROM BOVINE AORTA