The interaction of yeast citrate synthase with yeast mitochondrial inner membranes

L. G. Brent, P. Srere

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The specific interaction of yeast citrate synthase with yeast mitochondrial inner membranes was characterized with respect to saturability of binding, pH optimum, effect of ionic strength, temperature response, and inhibition by oxalacetate. The binding ability of the inner membranes is inhibited by proteolysis and heat treatment, which implies that the membrane component(s) responsible for binding is a protein. A protein fraction from inner membranes when added to liposomes will bind citrate synthase. In addition, the binding of yeast fumarase, mitochondrial malate dehydrogenase, and cytosolic malate dehydrogenase to yeast inner membranes was examined. For these studies the yeast mitochondrial matrix enzymes, citrate synthase (from two types of yeast), malate dehydrogenase, and fumarase, as well as cytosolic malate dehydrogenase, were purified using rapid new techniques.

Original languageEnglish
Pages (from-to)319-325
Number of pages7
JournalJournal of Biological Chemistry
Volume262
Issue number1
Publication statusPublished - 1987

Fingerprint

Citrate (si)-Synthase
Mitochondrial Membranes
Yeast
Malate Dehydrogenase
Yeasts
Membranes
Fumarate Hydratase
Proteolysis
Ionic strength
Liposomes
Osmolar Concentration
Proteins
Hot Temperature
Heat treatment
Temperature
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

The interaction of yeast citrate synthase with yeast mitochondrial inner membranes. / Brent, L. G.; Srere, P.

In: Journal of Biological Chemistry, Vol. 262, No. 1, 1987, p. 319-325.

Research output: Contribution to journalArticle

@article{1b3e2892d61b4880951f373c91bef29d,
title = "The interaction of yeast citrate synthase with yeast mitochondrial inner membranes",
abstract = "The specific interaction of yeast citrate synthase with yeast mitochondrial inner membranes was characterized with respect to saturability of binding, pH optimum, effect of ionic strength, temperature response, and inhibition by oxalacetate. The binding ability of the inner membranes is inhibited by proteolysis and heat treatment, which implies that the membrane component(s) responsible for binding is a protein. A protein fraction from inner membranes when added to liposomes will bind citrate synthase. In addition, the binding of yeast fumarase, mitochondrial malate dehydrogenase, and cytosolic malate dehydrogenase to yeast inner membranes was examined. For these studies the yeast mitochondrial matrix enzymes, citrate synthase (from two types of yeast), malate dehydrogenase, and fumarase, as well as cytosolic malate dehydrogenase, were purified using rapid new techniques.",
author = "Brent, {L. G.} and P. Srere",
year = "1987",
language = "English",
volume = "262",
pages = "319--325",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "1",

}

TY - JOUR

T1 - The interaction of yeast citrate synthase with yeast mitochondrial inner membranes

AU - Brent, L. G.

AU - Srere, P.

PY - 1987

Y1 - 1987

N2 - The specific interaction of yeast citrate synthase with yeast mitochondrial inner membranes was characterized with respect to saturability of binding, pH optimum, effect of ionic strength, temperature response, and inhibition by oxalacetate. The binding ability of the inner membranes is inhibited by proteolysis and heat treatment, which implies that the membrane component(s) responsible for binding is a protein. A protein fraction from inner membranes when added to liposomes will bind citrate synthase. In addition, the binding of yeast fumarase, mitochondrial malate dehydrogenase, and cytosolic malate dehydrogenase to yeast inner membranes was examined. For these studies the yeast mitochondrial matrix enzymes, citrate synthase (from two types of yeast), malate dehydrogenase, and fumarase, as well as cytosolic malate dehydrogenase, were purified using rapid new techniques.

AB - The specific interaction of yeast citrate synthase with yeast mitochondrial inner membranes was characterized with respect to saturability of binding, pH optimum, effect of ionic strength, temperature response, and inhibition by oxalacetate. The binding ability of the inner membranes is inhibited by proteolysis and heat treatment, which implies that the membrane component(s) responsible for binding is a protein. A protein fraction from inner membranes when added to liposomes will bind citrate synthase. In addition, the binding of yeast fumarase, mitochondrial malate dehydrogenase, and cytosolic malate dehydrogenase to yeast inner membranes was examined. For these studies the yeast mitochondrial matrix enzymes, citrate synthase (from two types of yeast), malate dehydrogenase, and fumarase, as well as cytosolic malate dehydrogenase, were purified using rapid new techniques.

UR - http://www.scopus.com/inward/record.url?scp=0023127748&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023127748&partnerID=8YFLogxK

M3 - Article

C2 - 3539936

AN - SCOPUS:0023127748

VL - 262

SP - 319

EP - 325

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 1

ER -