Disease relevance of

• Wild-type and mutant forms of bacteriorhodopsin (sbR) from Halobacterium salinarium, produced by Escherichia coli overexpression of a synthetic gene, were reversibly unfolded in 1, 2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC), 3-[(3-cholamidopropyl)dimethylamino]-2-hydroxyl-1-propane (CHAPSO), and sodium dodecyl sulfate (SDS) mixed micelles [1].

High impact information on

• CXCR4 was found to multimerize in cell lysates containing the detergents CHAPSO or Cymal-7 but not other detergents that have been shown to disrupt the native conformation of CXCR4 [2].
• Purple membrane was solubilized in Triton X-100 and BR was purified by size exclusion chromatography using 3-[cholamidopropyl)dimethylammonio]-2-hydroxyl-1-propanesulfonic acid (CHAPSO) detergent at pH 5 [3].
• The muscarinic receptor from the cerebral cortex, heart, and lacrimal gland can be solubilized in the zwitterionic detergent 3-(3-cholamidopropyl)dimethylammonio-2-hydroxy-1-propane sulfonate (CHAPSO) with retention of high affinity [3H]N-methyls-copolamine binding [4].
• These inhibitor derivatives bound and precipitated PS1 fragments from membrane CHAPSO extracts [5].
• Our experiments provide the basis for studying the thermodynamic stability of sbR by evaluating reversible folding and unfolding conditions in DMPC/CHAPSO/SDS mixed micelles [1].

Biological context of

• The photocycle kinetics for BR purified from each mutant are determined for micellar solutions in two detergents, nonyl glucoside and CHAPSO, and are compared to results from studies on delipidated BR (d-BR) in the same detergents [6].
• Functional binding sites for [125I]IAPP and [125I]CGRP were solubilized from rat lung membranes with CHAPSO (10 mM) [7].

Anatomical context of

• Dopamine receptor binding proteins were solubilized with the detergent 3-(3-cholamidopropyl) dimethylammonio-2-hydroxy-1-propanesulfonate (CHAPSO) from bovine and rat striatal membranes [8].
• Disruption of the microsomes by Chapso or by ultrasonication markedly enhanced the thermolability of the mannose-6-phosphatase activity [9].
• A specific receptor for the brain-gut neuropeptide pituitary adenylate-cyclase-activating polypeptide (PACAP-1 receptor) was solubilized with Chapso from porcine brain plasma membranes and purified [10].
• Complete disruption of rat liver microsomes was achieved by incubation for 60 min at 0 degree C in the presence of 4 mM zwitterionic detergent 3-[(3-cholamido-propyl)dimethyl-ammonio]-2-hydroxy-1-propane sulphonate (Chapso) [9].
• Functional 3 beta-hydroxysteroid dehydrogenase coupled with isomerase (3 beta-HSD) was extracted from dog pancreatic mitochondria by treatment with the zwitterionic detergent CHAPSO [11].

Associations of with other chemical compounds

• This paper describes a study undertaken to assess the possibility and practical consequences of reconstituting integral and peripheral membrane proteins into bilayered discoidal mixed micelles ("bicelles") composed of dimyristoylphosphatidylcholine and smaller amounts of either CHAPSO or short-chain phosphatidylcholine [12].
• The measured rate of flash-induced MII formation decreases by a factor of 300 from n-dodecyl-beta-D-maltoside (k = 4 x 10(3) at 18 degrees C, pH 6.5), over (3-(lauroyloxy)propyl)-phosphorylcholine (deoxylysolecithin), n-octyl-beta-D-glucopyranoside, sodium cholate to Chapso [13].
• This phenomenon was used to determine the concentration of the zwitterionic detergents CHAPS, CHAPSO, and sulfobetaine SB-12 in solution by titration with ammonium sulfate in the presence of Triton X-100 [14].

Gene context of

• Alzheimer amyloid precursor aspartyl proteinase activity in CHAPSO homogenates of Spodoptera frugiperda cells [15].
• The detergents, SDS and Chapso, consistently dissociated several major proteins (Mr 20, 40, 66 and over 200 kd) from opsonized RRBC [16].
• The production of 19-nor was not restricted to the CHAPSO-soluble protein fraction of kidney mitochondria but was also found in both the CHAPSO-soluble and -insoluble fractions of chick liver mitochondria and CHAPSO-treated bovine serum albumin (BSA) [17].

Analytical, diagnostic and therapeutic context of

• It was observed that the plots of CSA or dipolar coupling versus overall bilayer order obtained from DHPC and CHAPSO titrations were linear [18].
• Analysis of PS1 complexes by blue native gel electrophoresis and western blotting indicated that the CHAPSO extracts contained complexes of approximately 900, 500, and 400 kDa [5].

References