Diffusion-In-Gel Methods for Immunological Analysis II (Part 1 of 4)

Ouchterlony, Örjan

doi:10.1159/000313795

Cited by 1,223 publications

(59 citation statements)

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“…The extent of agglutination was observed by a Leitz phase-contrast microscope at a magnification of 400. Double immunodiffusion test in 1 agar platzs was performed according to Ouchterlony [36]. The gels were prepared in 0.01 M tricine/NaOH, pH 7.5, 0.15 M NaCl and 0.05 NaN3.…”

Section: Methodsmentioning

confidence: 99%

Antibodies to the F₁‐ATPase of Rhodospirillum rubrum and Its Purified Native β‐Subunit:

Philosoph¹,

Gromet-Elhanan²

1981

European Journal of Biochemistry

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1 . Antibodies prepared against the Rhodospirillunt ruhrum F1-ATPase (RrFI) and its purified, native [hubunit, exhibited cross-reactivity with thc following soluble preparations of R. ruhrunt ATPase: RrFo . FI, RrFl and thc 8-subunit. Anti-RrF1, but not anti-l) antibodies, also formed precipitin lines with soluble @-less RrFl, indicating that antigenic determinants of both the 1-subunit and the other four RrFl-subunits are expressed in the whole RrFl molecule. Both antibodies agglutinated the R. rubvum chromatophores, suggesting that the [hubunit is located on the external part of RrF1.2. Both antibodies inhibited ATP synthesis and hydrolysis activities of R. rubrum chromatophores, as well a s all the soluble ATPase reactions. Similar concentrations of each antibody were required for 50 inhibition of all these reactions, but anti-RrFI was always somewhat more effective than anti-P. These data indicate that the []-subunit is involved in the catalytic site of the RrFl-enzyme.3. The antibodies prepared against R. rubrum F1-ATPase and its P-subunit could bind thc soluble chloroplast F1-ATPase (CF1) and inhibited ATP-linked reactions carried out by chloroplasts and by soluble CFI. In these reactions, unlike in the R. rubrun? ones, anti-@ was a more potent inhibitor than the anti-RrF1 antibody.The cross-reaction obtained between the antibodies raised against R. rubrurn F1 and its b-subunit and the chloroplast CF1 indicates the presence of similar antigenic determinants in the photosynthetic prokaryotic and eukaryotic F1-ATPases, which have been conserved during evolution.

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Section: Methodsmentioning

confidence: 99%

Antibodies to the F₁‐ATPase of Rhodospirillum rubrum and Its Purified Native β‐Subunit:

Philosoph¹,

Gromet-Elhanan²

1981

European Journal of Biochemistry

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“…The polyclonal aIitise- rum prepared against the CSase mixture was tested by Ouchterlony double immunodiffusion analysis. 20) As shown in Fig. 1, the precipitin lines were completely fused, indicating that the antigens have identical epitopes.…”

Section: Resultsmentioning

confidence: 80%

Physiological Study of Cysteine Synthase Isozymes inSpinacia oleraceaSeedlings

Yamaguchi

Zhu

et al. 1996

Bioscience, Biotechnology, and Biochemistry

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“…Human fetal c-FABP, antibodies against human placenta pl-6.9 FABP and human fetal hFABP were prepared in our laboratory [17,23,24]. Immunological cross-reactivity of human placenta FABP was tested by Ouchterlony double-immunodiffusion test [25].…”

Section: Immunological Methodsmentioning

confidence: 99%

Characterization of cardiac fatty‐acid‐binding protein from human placenta

Das

Mukherjea

1993

European Journal of Biochemistry

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When a 105000Xg supernatant of human placenta was incubated with [l-I4C]oleate and subjected to Sephadex G-75 gel filtration and HPLC, two fatty-acid-binding protein (FABP) peaks were obtained. One of these, when further purified by carboxymethyl-cellulose, gave one 15.3-kDa FABP with pZ5.3. The other, when chromatographed on DEAE cellulose, separated into two 14.2-M)a FABP with pZ 6.9 and 5.4. Purity of the proteins was checked by SDS/PAGE. Molecular mass, pZ, immunochemical properties and amino acid compositions all indicated that 15.3-kDa FABP was of the cardiac type, whereas both 14.2-kDa FABP were of the hepatic type. Cardiac FABP did not cross-react with hepatic proteins. When tested for the acceptor/donor properties of these FABP, hepatic types were found to be better candidates than cardiac in uptaking fatty acids from liposomes. Cardiac FABP, on the other hand, acted in a more efficient way as a donor, indicating a distinct role of these proteins in human placenta, which furnishes a multiorgan system for the developing fetus.Fatty-acid-binding proteins (FABP) are found in extraordinary abundance in various mammalian tissues that are involved in uptake andfutilization of fatty acids [l, 21. These proteins belong to a new superfamily of 14-16 kDa nonenzymic cytosolic proteins which are characterized by structural similarity, indicating a common ancestral gene [3, 41. In addition to FABP, this protein family includes the various cellular retinoid-binding proteins, the p2 protein of periferal nerve myelin and the p422 adipocyte protein [5-71. Recently, two new proteins, bovine mammary-derived growth inhibitor, a proposed growth inhibitor and gastrotropin, a putative stimulator of gastric acid and pepsinogen secretion, have been shown to belong to this family, extending the similarity in an unexpected way [8, 91. Of all FABP reported so far, perhaps the most extensively studied are hepatic (h), cardiac (c) and gut (g) types [l]. Although the precise physiological role of these proteins is yet to be elucidated, the proposed functions include promoting the cellular uptake and intracellular utilization of fatty acids, targeting fatty acids and acyl-CoA to different metabolic pathways, modulating enzyme activities and protecting enzymes and cellular structures from detergent effects. FABP have tissue-specific expression with some tissues containing more than one type [lo, 111. Each of these proteins may thus be adapted to serve a unique physiological role in one organ according to tissue needs.During embryogenesis, free fatty acids are transported across the placenta from mother to fetus and vice versa [12, 131. In addition, both fatty acid synthesis [14] and oxidation Correspondence to M. Mukherjea,

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Diffusion-In-Gel Methods for Immunological Analysis II (Part 1 of 4)

Cited by 1,223 publications

References 0 publications

Antibodies to the F₁‐ATPase of Rhodospirillum rubrum and Its Purified Native β‐Subunit:

Antibodies to the F₁‐ATPase of Rhodospirillum rubrum and Its Purified Native β‐Subunit:

Physiological Study of Cysteine Synthase Isozymes inSpinacia oleraceaSeedlings

Characterization of cardiac fatty‐acid‐binding protein from human placenta

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Diffusion-In-Gel Methods for Immunological Analysis II (Part 1 of 4)

Cited by 1,223 publications

References 0 publications

Antibodies to the F1‐ATPase of Rhodospirillum rubrum and Its Purified Native β‐Subunit:

Antibodies to the F1‐ATPase of Rhodospirillum rubrum and Its Purified Native β‐Subunit:

Physiological Study of Cysteine Synthase Isozymes inSpinacia oleraceaSeedlings

Characterization of cardiac fatty‐acid‐binding protein from human placenta

Contact Info

Product

Resources

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Antibodies to the F₁‐ATPase of Rhodospirillum rubrum and Its Purified Native β‐Subunit:

Antibodies to the F₁‐ATPase of Rhodospirillum rubrum and Its Purified Native β‐Subunit: