Isolation of chromaffin cell thapsigargin-sensitive Ca2+ store in light microsomes from bovine adrenal medulla |
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Institution: | 1. Department of Cardiology, Tel Aviv Medical Center, Israel;2. Department of Cardiology, Meir Medical Center, Kfar Saba, Israel;1. AIT Austrian Institute of Technology, Donau-City-Straße 1, 1220 Vienna, Austria;2. SBA Research, Favoritenstraße 16, 1040 Vienna, Austria;1. College of Computer Science and Technology, Jilin University, Changchun 130012, China;2. Key Laboratory of Symbolic Computation and Knowledge Engineering of Ministry of Education, Jilin University, Changchun, 130012, China;3. School of Mathematics, Jilin University, Changchun 130012, China |
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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.
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