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Isolation of chromaffin cell thapsigargin-sensitive Ca2+ store in light microsomes from bovine adrenal medulla

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Isolation of chromaffin cell thapsigargin-sensitive Ca2+ store in light microsomes from bovine adrenal medulla. / Mathiasen, D.; Røssum, L. M.; Robinson, I. M. et al.
In: International Journal of Biochemistry, Vol. 25, No. 5, 31.05.1993, p. 641-652.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Mathiasen, D, Røssum, LM, Robinson, IM, Burgoyne, RD, East, JM, Møller, M, Rasmussen, HN & Treiman, M 1993, 'Isolation of chromaffin cell thapsigargin-sensitive Ca2+ store in light microsomes from bovine adrenal medulla', International Journal of Biochemistry, vol. 25, no. 5, pp. 641-652. https://doi.org/10.1016/0020-711X(93)90348-I

APA

Mathiasen, D., Røssum, L. M., Robinson, I. M., Burgoyne, R. D., East, J. M., Møller, M., Rasmussen, H. N., & Treiman, M. (1993). Isolation of chromaffin cell thapsigargin-sensitive Ca2+ store in light microsomes from bovine adrenal medulla. International Journal of Biochemistry, 25(5), 641-652. https://doi.org/10.1016/0020-711X(93)90348-I

Vancouver

Mathiasen D, Røssum LM, Robinson IM, Burgoyne RD, East JM, Møller M et al. Isolation of chromaffin cell thapsigargin-sensitive Ca2+ store in light microsomes from bovine adrenal medulla. International Journal of Biochemistry. 1993 May 31;25(5):641-652. doi: 10.1016/0020-711X(93)90348-I

Author

Mathiasen, D. ; Røssum, L. M. ; Robinson, I. M. et al. / Isolation of chromaffin cell thapsigargin-sensitive Ca2+ store in light microsomes from bovine adrenal medulla. In: International Journal of Biochemistry. 1993 ; Vol. 25, No. 5. pp. 641-652.

Bibtex

@article{2e537d605f4b405fb73780bbd22e31c3,
title = "Isolation of chromaffin cell thapsigargin-sensitive Ca2+ store in light microsomes from bovine adrenal medulla",
abstract = "1. 1. A subcellular fractionation procedure for bovine adrenal glands was designed with the aim to study the biochemical properties of Ca2+ stores in chromaffin cells. 2. 2. The thapsigargin-sensitive compartment of Ca2+ stores was found to be highly enriched in a light microsomal fraction (LMF) on a 15-30% linear sucrose gradient, and was found to be essentially devoid of contamination by plasma, mitochondrial or secretory granule membranes. 3. 3. A Ca2+-pumping ATPase was identified in this LMF as a 97 kDa protein forming an acid-stable, Ca2+-dependent, thapsigargin-sensitive phosphorylated intermediate upon incubation with [γ-32P]ATP, suggesting this protein to represent a SERCA-3 isoform of Ca2+ ATPases. 4. 4. A major 162 kDa protein, previously demonstrated in the isolated chromaffin cells, was enriched in the LMF, distributing on sucrose gradients in parallel with the thapsigargin-sensitive Ca2+ uptake. 5. 5. LMF appears to represent a part of the thapsigargin-sensitive Ca2+ store of chromaffin cells, and should be useful for further studies of the store properties at the subcellular and molecular level.",
author = "D. Mathiasen and R{\o}ssum, {L. M.} and Robinson, {I. M.} and Burgoyne, {R. D.} and East, {J. M.} and M. M{\o}ller and Rasmussen, {H. N.} and M. Treiman",
year = "1993",
month = may,
day = "31",
doi = "10.1016/0020-711X(93)90348-I",
language = "English",
volume = "25",
pages = "641--652",
journal = "International Journal of Biochemistry",
issn = "0020-711X",
publisher = "Pergamon Press Ltd.",
number = "5",

}

RIS

TY - JOUR

T1 - Isolation of chromaffin cell thapsigargin-sensitive Ca2+ store in light microsomes from bovine adrenal medulla

AU - Mathiasen, D.

AU - Røssum, L. M.

AU - Robinson, I. M.

AU - Burgoyne, R. D.

AU - East, J. M.

AU - Møller, M.

AU - Rasmussen, H. N.

AU - Treiman, M.

PY - 1993/5/31

Y1 - 1993/5/31

N2 - 1. 1. A subcellular fractionation procedure for bovine adrenal glands was designed with the aim to study the biochemical properties of Ca2+ stores in chromaffin cells. 2. 2. The thapsigargin-sensitive compartment of Ca2+ stores was found to be highly enriched in a light microsomal fraction (LMF) on a 15-30% linear sucrose gradient, and was found to be essentially devoid of contamination by plasma, mitochondrial or secretory granule membranes. 3. 3. A Ca2+-pumping ATPase was identified in this LMF as a 97 kDa protein forming an acid-stable, Ca2+-dependent, thapsigargin-sensitive phosphorylated intermediate upon incubation with [γ-32P]ATP, suggesting this protein to represent a SERCA-3 isoform of Ca2+ ATPases. 4. 4. A major 162 kDa protein, previously demonstrated in the isolated chromaffin cells, was enriched in the LMF, distributing on sucrose gradients in parallel with the thapsigargin-sensitive Ca2+ uptake. 5. 5. LMF appears to represent a part of the thapsigargin-sensitive Ca2+ store of chromaffin cells, and should be useful for further studies of the store properties at the subcellular and molecular level.

AB - 1. 1. A subcellular fractionation procedure for bovine adrenal glands was designed with the aim to study the biochemical properties of Ca2+ stores in chromaffin cells. 2. 2. The thapsigargin-sensitive compartment of Ca2+ stores was found to be highly enriched in a light microsomal fraction (LMF) on a 15-30% linear sucrose gradient, and was found to be essentially devoid of contamination by plasma, mitochondrial or secretory granule membranes. 3. 3. A Ca2+-pumping ATPase was identified in this LMF as a 97 kDa protein forming an acid-stable, Ca2+-dependent, thapsigargin-sensitive phosphorylated intermediate upon incubation with [γ-32P]ATP, suggesting this protein to represent a SERCA-3 isoform of Ca2+ ATPases. 4. 4. A major 162 kDa protein, previously demonstrated in the isolated chromaffin cells, was enriched in the LMF, distributing on sucrose gradients in parallel with the thapsigargin-sensitive Ca2+ uptake. 5. 5. LMF appears to represent a part of the thapsigargin-sensitive Ca2+ store of chromaffin cells, and should be useful for further studies of the store properties at the subcellular and molecular level.

U2 - 10.1016/0020-711X(93)90348-I

DO - 10.1016/0020-711X(93)90348-I

M3 - Journal article

C2 - 8349007

AN - SCOPUS:0027196889

VL - 25

SP - 641

EP - 652

JO - International Journal of Biochemistry

JF - International Journal of Biochemistry

SN - 0020-711X

IS - 5

ER -