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Binding of Amyloid Beta-Protein to Intracellular Brain Proteins in Rat and Human (1998)

Ray, I. ; Chauhan, A. ; Wisniewski, H. M. ; [et al.]

Springer

Neurochemical research 23 (1998), S. 1277-1282

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ISSN: 1573-6903

Keywords: Amyloid beta protein ; Alzheimer's disease ; Aβ binding proteins ; intracellular brain proteins

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract Amyloid beta-protein (Aβ), in its soluble form, is known to bind several circulatory proteins such as apolipoprotein (apo) E, apo J and transthyretin. However, the binding of Aβ to intracellular proteins has not been studied. We have developed an overlay assay to study Aβ binding to intracellular brain proteins. The supernatants from both rat and human brains were found to contain several proteins that bind to Aβ 1–40 and Aβ 1–42. No major difference was observed in the Aβ binding-proteins from brain supernatants of patients with Alzheimer's disease and normal age-matched controls. Binding studies using shorter amyloid beta-peptides and competitive overlay assays showed that the binding site of Aβ to brain proteins resides between 12–28 amino acid sequence of Aβ. The presence of several intracellular Aβ-binding (AβB) proteins suggests that these proteins may either protect Aβ from its fibrillization or alternatively promote Aβ polymerization. Identification of these proteins and their binding affinities for Aβ are needed to assess their potential role in the pathogenesis of Alzheimer's disease.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1023/A:1020744216699

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Chelate Formation between Iron(III) and o-Cresotic Acid; a Spectrophotometric Study (1963)

Katiyar, Sarvagya S. ; Chauhan, V. B. S.

Weinheim : Wiley-Blackwell

Zeitschrift für anorganische Chemie 323 (1963), S. 28-34

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ISSN: 0044-2313

Keywords: Chemistry ; Inorganic Chemistry

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Description / Table of Contents: Zusammensetzung und Stabilität der aus Fe37+ und o-Kresotinsäure gebildeten blauvioletten Chelatverbindung wurden spektrophotometrisch bei αDmax = 550 mμ ermittelt. Es ist ein 1 : 1-Komplex, für dessen Beständigkeitskonstante bei 35,5°C und pH 1,93; 2,90 und 3,92 folgende Werte erhalten wurden: log k = 4,61; 4,15 bzw. 3,40.

Notes: The formation of a bluish violet chelate between iron(III) and o-cresotic acid with absorption maximum at 550 mμ has been observed. The composition of the chelate has been determined spectrophotometrically using methods of continuous variation, slope ratio and mole-ratio; the ratio of iron(III) to o-cresotate corresponded to 1 : 1. These data were further utilised for the computation of stability constant (log k) at pH 1.93, 2.90 and 3.92, which at 35.5°C worked out to be 4.61, 4.15 and 3.40 respectively.

Additional Material: 7 Ill.