Lectins as probes of chromatin structure. Binding of concanavalin A to purified rat liver chromatin

W. B. Rizzo, M. Bustin

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Concanavalin A (Con A) binds specifically to rat liver chromatin. The extent of binding is directly proportional to both chromatin and concanavalin A concentration. It is reversible and inhibited by specific sugars for which concanavalin A has a binding site. Scatchard analysis reveals the presence of one type of Con A-binding site, with an apparent dissociation constant of 3x10-7M. A maximum of 10 pmol of Con A binds to 10 μg of chromatin, indicating an average of one binding site/1400 base pairs of DNA. To identify the polypeptide chains which contain Con A-binding sites, chromosomal proteins were separated by electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate. Con A receptors were localized by incubating the gel in 125I-Con A and subsequent autoradiography. Three major polypeptide bands which bind Con A were identified among the nonhistone chromosomal proteins. The apparent molecular weights of these glycoproteins are 135,000, 125,000, and 69,000. We suggest that lectins may serve as probes for the study of the organization of specific components in chromatin.

Original languageEnglish (US)
Pages (from-to)7062-7067
Number of pages6
JournalJournal of Biological Chemistry
Volume252
Issue number20
StatePublished - Dec 1 1977

Fingerprint

Concanavalin A
Lectins
Liver
Chromatin
Rats
Concanavalin A Receptors
Non Histone Chromosomal Proteins
Binding Sites
Peptides
Electrophoresis
Autoradiography
Sugars
Base Pairing
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Glycoproteins
Molecular Weight
Gels
Molecular weight
DNA

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Lectins as probes of chromatin structure. Binding of concanavalin A to purified rat liver chromatin. / Rizzo, W. B.; Bustin, M.

In: Journal of Biological Chemistry, Vol. 252, No. 20, 01.12.1977, p. 7062-7067.

Research output: Contribution to journalArticle

@article{05dfb1fdea794563a0cd6c3a11b4776a,
title = "Lectins as probes of chromatin structure. Binding of concanavalin A to purified rat liver chromatin",
abstract = "Concanavalin A (Con A) binds specifically to rat liver chromatin. The extent of binding is directly proportional to both chromatin and concanavalin A concentration. It is reversible and inhibited by specific sugars for which concanavalin A has a binding site. Scatchard analysis reveals the presence of one type of Con A-binding site, with an apparent dissociation constant of 3x10-7M. A maximum of 10 pmol of Con A binds to 10 μg of chromatin, indicating an average of one binding site/1400 base pairs of DNA. To identify the polypeptide chains which contain Con A-binding sites, chromosomal proteins were separated by electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate. Con A receptors were localized by incubating the gel in 125I-Con A and subsequent autoradiography. Three major polypeptide bands which bind Con A were identified among the nonhistone chromosomal proteins. The apparent molecular weights of these glycoproteins are 135,000, 125,000, and 69,000. We suggest that lectins may serve as probes for the study of the organization of specific components in chromatin.",
author = "Rizzo, {W. B.} and M. Bustin",
year = "1977",
month = "12",
day = "1",
language = "English (US)",
volume = "252",
pages = "7062--7067",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "20",

}

TY - JOUR

T1 - Lectins as probes of chromatin structure. Binding of concanavalin A to purified rat liver chromatin

AU - Rizzo, W. B.

AU - Bustin, M.

PY - 1977/12/1

Y1 - 1977/12/1

N2 - Concanavalin A (Con A) binds specifically to rat liver chromatin. The extent of binding is directly proportional to both chromatin and concanavalin A concentration. It is reversible and inhibited by specific sugars for which concanavalin A has a binding site. Scatchard analysis reveals the presence of one type of Con A-binding site, with an apparent dissociation constant of 3x10-7M. A maximum of 10 pmol of Con A binds to 10 μg of chromatin, indicating an average of one binding site/1400 base pairs of DNA. To identify the polypeptide chains which contain Con A-binding sites, chromosomal proteins were separated by electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate. Con A receptors were localized by incubating the gel in 125I-Con A and subsequent autoradiography. Three major polypeptide bands which bind Con A were identified among the nonhistone chromosomal proteins. The apparent molecular weights of these glycoproteins are 135,000, 125,000, and 69,000. We suggest that lectins may serve as probes for the study of the organization of specific components in chromatin.

AB - Concanavalin A (Con A) binds specifically to rat liver chromatin. The extent of binding is directly proportional to both chromatin and concanavalin A concentration. It is reversible and inhibited by specific sugars for which concanavalin A has a binding site. Scatchard analysis reveals the presence of one type of Con A-binding site, with an apparent dissociation constant of 3x10-7M. A maximum of 10 pmol of Con A binds to 10 μg of chromatin, indicating an average of one binding site/1400 base pairs of DNA. To identify the polypeptide chains which contain Con A-binding sites, chromosomal proteins were separated by electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate. Con A receptors were localized by incubating the gel in 125I-Con A and subsequent autoradiography. Three major polypeptide bands which bind Con A were identified among the nonhistone chromosomal proteins. The apparent molecular weights of these glycoproteins are 135,000, 125,000, and 69,000. We suggest that lectins may serve as probes for the study of the organization of specific components in chromatin.

UR - http://www.scopus.com/inward/record.url?scp=0017751235&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017751235&partnerID=8YFLogxK

M3 - Article

C2 - 903351

AN - SCOPUS:0017751235

VL - 252

SP - 7062

EP - 7067

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 20

ER -