Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages.

H. L. Yin, T. P. Stossel

Research output: Contribution to journalArticle

122 Citations (Scopus)

Abstract

We describe the purification procedure and some of the physiochemical properties of gelsolin, a major Ca2+-dependent regulatory protein of actin gel-sol transformation in rabbit lung macrophages. Gelsolin accounts for the majority of Ca2+ control of actin gelation in macrophage extracts. It is a single polypeptide chain with an average molecular weight of 91,000 a Stokes radius of 44 A, a sedimentation coefficient (s20(0),w) of 4.9 S, an isoelectric point of 6.1, and a frictional ratio of 1.43. Gelsolin binds 2 mol of Ca2+ with high affinity (Ka 1.09 X 10(6) M-1) in the presence of 0.1 M KCl and 2 mM MgCl2.

Original languageEnglish (US)
Pages (from-to)9490-9493
Number of pages4
JournalJournal of Biological Chemistry
Volume255
Issue number19
StatePublished - Oct 10 1980

Fingerprint

Gelsolin
Macrophages
Purification
Structural properties
Actins
Proteins
Magnesium Chloride
Isoelectric Point
Polymethyl Methacrylate
Gelation
Sedimentation
Molecular Weight
Gels
Molecular weight
Rabbits
Lung
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages. / Yin, H. L.; Stossel, T. P.

In: Journal of Biological Chemistry, Vol. 255, No. 19, 10.10.1980, p. 9490-9493.

Research output: Contribution to journalArticle

@article{5b3fcfcb7ab84957aa4dae5444b80ac8,
title = "Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages.",
abstract = "We describe the purification procedure and some of the physiochemical properties of gelsolin, a major Ca2+-dependent regulatory protein of actin gel-sol transformation in rabbit lung macrophages. Gelsolin accounts for the majority of Ca2+ control of actin gelation in macrophage extracts. It is a single polypeptide chain with an average molecular weight of 91,000 a Stokes radius of 44 A, a sedimentation coefficient (s20(0),w) of 4.9 S, an isoelectric point of 6.1, and a frictional ratio of 1.43. Gelsolin binds 2 mol of Ca2+ with high affinity (Ka 1.09 X 10(6) M-1) in the presence of 0.1 M KCl and 2 mM MgCl2.",
author = "Yin, {H. L.} and Stossel, {T. P.}",
year = "1980",
month = "10",
day = "10",
language = "English (US)",
volume = "255",
pages = "9490--9493",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "19",

}

TY - JOUR

T1 - Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages.

AU - Yin, H. L.

AU - Stossel, T. P.

PY - 1980/10/10

Y1 - 1980/10/10

N2 - We describe the purification procedure and some of the physiochemical properties of gelsolin, a major Ca2+-dependent regulatory protein of actin gel-sol transformation in rabbit lung macrophages. Gelsolin accounts for the majority of Ca2+ control of actin gelation in macrophage extracts. It is a single polypeptide chain with an average molecular weight of 91,000 a Stokes radius of 44 A, a sedimentation coefficient (s20(0),w) of 4.9 S, an isoelectric point of 6.1, and a frictional ratio of 1.43. Gelsolin binds 2 mol of Ca2+ with high affinity (Ka 1.09 X 10(6) M-1) in the presence of 0.1 M KCl and 2 mM MgCl2.

AB - We describe the purification procedure and some of the physiochemical properties of gelsolin, a major Ca2+-dependent regulatory protein of actin gel-sol transformation in rabbit lung macrophages. Gelsolin accounts for the majority of Ca2+ control of actin gelation in macrophage extracts. It is a single polypeptide chain with an average molecular weight of 91,000 a Stokes radius of 44 A, a sedimentation coefficient (s20(0),w) of 4.9 S, an isoelectric point of 6.1, and a frictional ratio of 1.43. Gelsolin binds 2 mol of Ca2+ with high affinity (Ka 1.09 X 10(6) M-1) in the presence of 0.1 M KCl and 2 mM MgCl2.

UR - http://www.scopus.com/inward/record.url?scp=0019321663&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019321663&partnerID=8YFLogxK

M3 - Article

VL - 255

SP - 9490

EP - 9493

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 19

ER -