Effect of chemical modification on the crystallization of Ca2+-ATPase in sarcoplasmic reticulum

Sandor Varga, P. Csermely, Nandor Mullner, L. Dux, Anthony Martonosi

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The influence of chemical modification on the morphology of crystalline ATPase aggregates was analyzed in sarcoplasmic reticulum (SR) vesicles. The Ca2+-ATPase forms monomer-type (P1) type crystals in the E1 and dimer-type (P2) crystals in the E2 conformation. The P1 type crystals are induced by Ca2+ or lanthanides; P2 type crystals are observed in Ca2+-free media in the presence of vanadate or inorganic phosphate. P1- and P2-type Ca2+-ATPase crystals do not coexist in significant amounts in native sarcoplasmic reticulum membrane. The crystallization of Ca2+-ATPase in the E2 conformation is inhibited by guanidino-group reagents (2,3-butanedione and phenylglyoxal), SH-group reagents, phospholipases C or A2, and detergents, together with inhibition of ATPase activity. Amino-group reagents (fluorescein 5′-isothiocyanate, pyridoxal phosphate and fluorescamine) inhibit ATPase activity but do not interfere with the crystallization of Ca2+-ATPase induced by vanadate. In fluorescamine-treated sarcoplasmic reticulum the vanadate-induced crystals contain significant P1-type regions in addition to the dominant P2 form.

Original languageEnglish
Pages (from-to)187-195
Number of pages9
JournalBBA - Biomembranes
Volume896
Issue number2
DOIs
Publication statusPublished - Jan 26 1987

Fingerprint

Calcium-Transporting ATPases
Chemical modification
Sarcoplasmic Reticulum
Crystallization
Vanadates
Fluorescamine
Adenosine Triphosphatases
Crystals
Phenylglyoxal
Diacetyl
Lanthanoid Series Elements
Sulfhydryl Reagents
Pyridoxal Phosphate
Conformations
Fluorescein-5-isothiocyanate
Phospholipases A2
Type C Phospholipases
Detergents
Phosphates
Dimers

Keywords

  • ATPase, Ca
  • Membrane cystal
  • Sarcoplasmic reticulum

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology

Cite this

Effect of chemical modification on the crystallization of Ca2+-ATPase in sarcoplasmic reticulum. / Varga, Sandor; Csermely, P.; Mullner, Nandor; Dux, L.; Martonosi, Anthony.

In: BBA - Biomembranes, Vol. 896, No. 2, 26.01.1987, p. 187-195.

Research output: Contribution to journalArticle

Varga, Sandor ; Csermely, P. ; Mullner, Nandor ; Dux, L. ; Martonosi, Anthony. / Effect of chemical modification on the crystallization of Ca2+-ATPase in sarcoplasmic reticulum. In: BBA - Biomembranes. 1987 ; Vol. 896, No. 2. pp. 187-195.
@article{8d57b462dd29417aaa418ad5d55c374f,
title = "Effect of chemical modification on the crystallization of Ca2+-ATPase in sarcoplasmic reticulum",
abstract = "The influence of chemical modification on the morphology of crystalline ATPase aggregates was analyzed in sarcoplasmic reticulum (SR) vesicles. The Ca2+-ATPase forms monomer-type (P1) type crystals in the E1 and dimer-type (P2) crystals in the E2 conformation. The P1 type crystals are induced by Ca2+ or lanthanides; P2 type crystals are observed in Ca2+-free media in the presence of vanadate or inorganic phosphate. P1- and P2-type Ca2+-ATPase crystals do not coexist in significant amounts in native sarcoplasmic reticulum membrane. The crystallization of Ca2+-ATPase in the E2 conformation is inhibited by guanidino-group reagents (2,3-butanedione and phenylglyoxal), SH-group reagents, phospholipases C or A2, and detergents, together with inhibition of ATPase activity. Amino-group reagents (fluorescein 5′-isothiocyanate, pyridoxal phosphate and fluorescamine) inhibit ATPase activity but do not interfere with the crystallization of Ca2+-ATPase induced by vanadate. In fluorescamine-treated sarcoplasmic reticulum the vanadate-induced crystals contain significant P1-type regions in addition to the dominant P2 form.",
keywords = "ATPase, Ca, Membrane cystal, Sarcoplasmic reticulum",
author = "Sandor Varga and P. Csermely and Nandor Mullner and L. Dux and Anthony Martonosi",
year = "1987",
month = "1",
day = "26",
doi = "10.1016/0005-2736(87)90179-9",
language = "English",
volume = "896",
pages = "187--195",
journal = "Biochimica et Biophysica Acta - Biomembranes",
issn = "0005-2736",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Effect of chemical modification on the crystallization of Ca2+-ATPase in sarcoplasmic reticulum

AU - Varga, Sandor

AU - Csermely, P.

AU - Mullner, Nandor

AU - Dux, L.

AU - Martonosi, Anthony

PY - 1987/1/26

Y1 - 1987/1/26

N2 - The influence of chemical modification on the morphology of crystalline ATPase aggregates was analyzed in sarcoplasmic reticulum (SR) vesicles. The Ca2+-ATPase forms monomer-type (P1) type crystals in the E1 and dimer-type (P2) crystals in the E2 conformation. The P1 type crystals are induced by Ca2+ or lanthanides; P2 type crystals are observed in Ca2+-free media in the presence of vanadate or inorganic phosphate. P1- and P2-type Ca2+-ATPase crystals do not coexist in significant amounts in native sarcoplasmic reticulum membrane. The crystallization of Ca2+-ATPase in the E2 conformation is inhibited by guanidino-group reagents (2,3-butanedione and phenylglyoxal), SH-group reagents, phospholipases C or A2, and detergents, together with inhibition of ATPase activity. Amino-group reagents (fluorescein 5′-isothiocyanate, pyridoxal phosphate and fluorescamine) inhibit ATPase activity but do not interfere with the crystallization of Ca2+-ATPase induced by vanadate. In fluorescamine-treated sarcoplasmic reticulum the vanadate-induced crystals contain significant P1-type regions in addition to the dominant P2 form.

AB - The influence of chemical modification on the morphology of crystalline ATPase aggregates was analyzed in sarcoplasmic reticulum (SR) vesicles. The Ca2+-ATPase forms monomer-type (P1) type crystals in the E1 and dimer-type (P2) crystals in the E2 conformation. The P1 type crystals are induced by Ca2+ or lanthanides; P2 type crystals are observed in Ca2+-free media in the presence of vanadate or inorganic phosphate. P1- and P2-type Ca2+-ATPase crystals do not coexist in significant amounts in native sarcoplasmic reticulum membrane. The crystallization of Ca2+-ATPase in the E2 conformation is inhibited by guanidino-group reagents (2,3-butanedione and phenylglyoxal), SH-group reagents, phospholipases C or A2, and detergents, together with inhibition of ATPase activity. Amino-group reagents (fluorescein 5′-isothiocyanate, pyridoxal phosphate and fluorescamine) inhibit ATPase activity but do not interfere with the crystallization of Ca2+-ATPase induced by vanadate. In fluorescamine-treated sarcoplasmic reticulum the vanadate-induced crystals contain significant P1-type regions in addition to the dominant P2 form.

KW - ATPase, Ca

KW - Membrane cystal

KW - Sarcoplasmic reticulum

UR - http://www.scopus.com/inward/record.url?scp=0023112391&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023112391&partnerID=8YFLogxK

U2 - 10.1016/0005-2736(87)90179-9

DO - 10.1016/0005-2736(87)90179-9

M3 - Article

VL - 896

SP - 187

EP - 195

JO - Biochimica et Biophysica Acta - Biomembranes

JF - Biochimica et Biophysica Acta - Biomembranes

SN - 0005-2736

IS - 2

ER -