Home LiteratureArticle Details

PMID: 6894235 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Band 4.1 causes spectrin-actin gels to become thixiotropic.

Biochemical and biophysical research communications ·Vol. 97 ·No. 4 ·1980-12-31 ·Pages 1429-35

Cohen CM, Korsgren C

Abstract

暂无摘要

MeSH Terms

Actins/metabolism Animals Blood Proteins/metabolism Cross-Linking Reagents Cytoskeletal Proteins Erythrocyte Membrane/metabolism Erythrocytes/metabolism Humans Kinetics Macromolecular Substances Membrane Proteins/metabolism Muscles/metabolism Neuropeptides Rabbits Spectrin/metabolism Viscosity

Chemicals

Actins Blood Proteins Cross-Linking Reagents Cytoskeletal Proteins Macromolecular Substances Membrane Proteins Neuropeptides erythrocyte membrane band 4.1 protein erythrocyte membrane protein band 4.1-like 1 Spectrin

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Cohen C M

Korsgren C

Article Info

Journal

Biochemical and biophysical research communications

Abbr.

Biochem Biophys Res Commun

ISSN

0006-291X

DOI

10.1016/s0006-291x(80)80025-8

Published

1980-12-31

Pages

1429-35

Language

English

Region

United States

NLM ID

0372516

Subset

Grants

NHLBI NIH HHS · HL24392 · United States

External Links

PubMed source DOI: 10.1016/s0006-291x(80)80025-8 View journal details

Analysis Services

Band 4.1 causes spectrin-actin gels to become thixiotropic.

Contact

WeChat Official Account