Immunological studies on the interaction of polyadenylic acid and human liver ribonuclease

Edward Neuwelt, William A. Gahl, Carl C. Levy

Research output: Contribution to journalArticle

Abstract

The effect of polyadenylic acid, a potent inhibitor of mammalian and bacterial RNAses, on the binding of human liver RNAse to its antibody was studied. To do this, a human liver RNAse antibody was immobilized on Sepharose 4B. Examination of the ability of the enzyme to bind to the immobilized anti-RNAse in the presence or absence of polyadenylic acid indicated that enzyme-antibody binding was more sensitive to the presence of polyadenylic acid than was enzyme activity. Furthermore, the effect of polyadenylic acid on enzyme-antibody binding was specific since neither polycytidylic acid nor polyuridylic acid had much effect on the antigenicity of the enzyme. The metal cation, Mg2+, and the polyamine, spermidine, but not putrescine, readily reversed the effects of polyadenylic acid on enzyme-antibody binding.

Original languageEnglish (US)
Pages (from-to)885-893
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume73
Issue number4
DOIs
StatePublished - Dec 20 1976
Externally publishedYes

Fingerprint

Poly A
Ribonucleases
Liver
Antibodies
Enzymes
Poly C
Poly U
Putrescine
Spermidine
Immobilized Antibodies
Polyamines
Enzyme activity
Sepharose
Cations
Metals

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Immunological studies on the interaction of polyadenylic acid and human liver ribonuclease. / Neuwelt, Edward; Gahl, William A.; Levy, Carl C.

In: Biochemical and Biophysical Research Communications, Vol. 73, No. 4, 20.12.1976, p. 885-893.

Research output: Contribution to journalArticle

@article{2cbd6d6fe6eb4e348ce4bd0793a264d3,
title = "Immunological studies on the interaction of polyadenylic acid and human liver ribonuclease",
abstract = "The effect of polyadenylic acid, a potent inhibitor of mammalian and bacterial RNAses, on the binding of human liver RNAse to its antibody was studied. To do this, a human liver RNAse antibody was immobilized on Sepharose 4B. Examination of the ability of the enzyme to bind to the immobilized anti-RNAse in the presence or absence of polyadenylic acid indicated that enzyme-antibody binding was more sensitive to the presence of polyadenylic acid than was enzyme activity. Furthermore, the effect of polyadenylic acid on enzyme-antibody binding was specific since neither polycytidylic acid nor polyuridylic acid had much effect on the antigenicity of the enzyme. The metal cation, Mg2+, and the polyamine, spermidine, but not putrescine, readily reversed the effects of polyadenylic acid on enzyme-antibody binding.",
author = "Edward Neuwelt and Gahl, {William A.} and Levy, {Carl C.}",
year = "1976",
month = "12",
day = "20",
doi = "10.1016/0006-291X(76)90205-9",
language = "English (US)",
volume = "73",
pages = "885--893",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",

}

TY - JOUR

T1 - Immunological studies on the interaction of polyadenylic acid and human liver ribonuclease

AU - Neuwelt, Edward

AU - Gahl, William A.

AU - Levy, Carl C.

PY - 1976/12/20

Y1 - 1976/12/20

N2 - The effect of polyadenylic acid, a potent inhibitor of mammalian and bacterial RNAses, on the binding of human liver RNAse to its antibody was studied. To do this, a human liver RNAse antibody was immobilized on Sepharose 4B. Examination of the ability of the enzyme to bind to the immobilized anti-RNAse in the presence or absence of polyadenylic acid indicated that enzyme-antibody binding was more sensitive to the presence of polyadenylic acid than was enzyme activity. Furthermore, the effect of polyadenylic acid on enzyme-antibody binding was specific since neither polycytidylic acid nor polyuridylic acid had much effect on the antigenicity of the enzyme. The metal cation, Mg2+, and the polyamine, spermidine, but not putrescine, readily reversed the effects of polyadenylic acid on enzyme-antibody binding.

AB - The effect of polyadenylic acid, a potent inhibitor of mammalian and bacterial RNAses, on the binding of human liver RNAse to its antibody was studied. To do this, a human liver RNAse antibody was immobilized on Sepharose 4B. Examination of the ability of the enzyme to bind to the immobilized anti-RNAse in the presence or absence of polyadenylic acid indicated that enzyme-antibody binding was more sensitive to the presence of polyadenylic acid than was enzyme activity. Furthermore, the effect of polyadenylic acid on enzyme-antibody binding was specific since neither polycytidylic acid nor polyuridylic acid had much effect on the antigenicity of the enzyme. The metal cation, Mg2+, and the polyamine, spermidine, but not putrescine, readily reversed the effects of polyadenylic acid on enzyme-antibody binding.

UR - http://www.scopus.com/inward/record.url?scp=0017042861&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017042861&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(76)90205-9

DO - 10.1016/0006-291X(76)90205-9

M3 - Article

C2 - 15625858

AN - SCOPUS:0017042861

VL - 73

SP - 885

EP - 893

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -