Isomerization reactions of charcoal-defatted bovine plasma albumin.  The N-F transition and acid expansion

Sogami, Masaru; Foster, Joseph F.

doi:10.1021/bi00846a020

Cited by 186 publications

(127 citation statements)

References 40 publications

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“…Moreover, their amino acid compositions are similar and their circular dichroic spectra in the far and the near UV are nearly identical. The circular dichroic properties are, in turn, very similar to those of other serum albumins (27,28,30,31).…”

Section: Discussionsupporting

confidence: 64%

Muscle beta-actinin and serum albumin of the chicken are indistinguishable by physicochemical and immunological criteria.

Heizman¹,

Müller²,

Jenny³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

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Chicken muscle ,B-actinin is considered to be one ofthe "true" myofibrillar components due to its specific binding to isolated myofibrils. Surprisingly, the direct comparison of this muscle protein with serum albumin, both isolated from chicken, showed that they behaved identically under several electrophoretic conditions. Furthermore, immunoreplica gels and doubleimmunodiffusion tests with antibodies prepared against 3-actinin established the serological identity of both proteins. No significant differences were found by circular dichroic spectroscopy or in amino acid composition. In addition, the amino-terminal sequences of both proteins were identical (H2N-Asp-Ala-Glu-HisLys-Ser-Glu-Ile-Ala-His-Arg-Tyr-Asn-Asp-Leu-). Combined, these results strongly indicate that, muscle ,B-actinin and serum albumin are similar, if not identical.There is a class ofminor myofibrillar components called actinins which were originally thought to be structurally related to actin (1, 2). Later, however, it became apparent that the physicochemical properties of the purified proteins were clearly different from those ofactin. Nevertheless, the name "actinin" has been retained because these proteins appear to interact directly with actin itself. At present, three different actinins, a, 13, and y, have been described (3-9).Among these, the status of,-actinin is the least clear, and two (ifnot three) proteins are currently designated as such. Two monomeric and possibly homologous proteins with molecular weights of60,000 and 65,000 have been isolated from rabbit and chicken muscle, respectively (10, 11). A third, dimeric protein (subunit molecular weights of 37,000 and 34,000), also designated ,3-actinin, was subsequently described by Maruyama et al. (12). Its relationship to the monomeric /3-actinin(s) is not understood and will therefore not be considered.Localization of the monomeric form(s) from both rabbit and chicken by indirect immunofluorescence revealed a strong and specific binding to the I region of isolated myofibrils (10, 11) and suggested involvement in the myofibrillar structure. Ultrastructural analysis more precisely demonstrated that the chicken protein was specifically oriented in two parallel stripes running transversely across the muscle fiber at the end of the thick filament-i.e., at the A/I junction (unpublished observation).In this work we present some unexpected results that indicate similarity (ifnot identity) ofthe structural muscle ,3-actinin with serum albumin. Both components, isolated from chicken, were found to be indistinguishable by electrophoresis in the presence or absence of NaDodSO4; their spectral properties, amino-terminal sequences, and immunological properties were also the same. MATERIALS AND METHODSProteins. Rabbit skeletal muscle actin, chicken ,3-actinin, and rabbit antibodies against chicken 13-actinin were prepared as described (11,(13)(14)(15) Amino-Terminal Sequences. The amino acid sequences were automatically determined with a Beckman sequencer model 890B (updated), with 4-N,N...

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Section: Discussionsupporting

confidence: 64%

Muscle beta-actinin and serum albumin of the chicken are indistinguishable by physicochemical and immunological criteria.

Heizman¹,

Müller²,

Jenny³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

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“…Furthermore, Leonard and Foster (37) showed that the pH profile of the N-F transition of BSA in acetic acid/acetate differs from that in chloride. In addition, the earlier onset of the N-F transition of the HSA used in our experiments could be due to differences in the preparation method, which is known to contribute to the structural behavior of albumin (38 -40) and/or to the absence of added salt and bound fatty acids, shifting the midpoint of the N-F transition of BSA to higher pH (41).…”

Section: Resultsmentioning

confidence: 98%

Conformational Transitions of the Three Recombinant Domains of Human Serum Albumin Depending on pH

Dockal¹,

Carter²,

Rüker³

2000

Journal of Biological Chemistry

431

323

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Human serum albumin (HSA) is a protein of 66.5 kDa that is composed of three homologous domains, each of which displays specific structural and functional characteristics. HSA is known to undergo different pH-dependent structural transitions, the N-F and F-E transitions in the acid pH region and the N-B transition at slightly alkaline pH. In order to elucidate the structural behavior of the recombinant HSA domains as standalone proteins and to investigate the molecular and structural origins of the pH-induced conformational changes of the intact molecule, we have employed fluorescence and circular dichroic methods. Here we provide evidence that the loosening of the HSA structure in the N-F transition takes place primarily in HSA-DOM III and that HSA-DOM I undergoes a structural rearrangement with only minor changes in secondary structure, whereas HSA-DOM II transforms to a molten globulelike state as the pH is reduced. In the pH region of the N-B transition of HSA, HSA-DOM I and HSA-DOM II experience a tertiary structural isomerization, whereas with HSA-DOM III no alterations in tertiary structure are observed, as judged from near-UV CD and fluorescence measurements.

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“…HSA (from Sigma-Aldrich, St. Louis, MO, USA) was essentially fatty acid free, according to the charcoal delipidation protocol [9][10][11] .0°C, were analyzed in the framework of the minimum three step-mechanism reported in Scheme 1 [8,[12][13][14][15], where HSA is the substrate-free protein, NphOAc is the substrate, HSA:NphOAc is the reversible protein-substrate complex, HSA-OAc is considered to be an ester formed between the acyl moiety of the substrate and the O atom of the Tyr411 phenoxyl group [8], AcOH is acetic acid, k +l is the second-order rate constant for the formation of the HSA:NphOAc complex starting from HSA and NphOAc, k À1 is the first-order rate constant for the dissociation of the HSA:NphOAc complex to HSA and NphOAc, K s (=k À1 /k +1 ) is the pre-equilibrium constant, k +2 is the first-order acylation rate constant, k À2 is the first-order rate constant for the conversion of HSA-OAc to HSA:NphOAc, k +3 is the first-order deacylation rate constant, and k À3 is the second-order rate constant for the formation of the HSA-OAc adduct starting from HSA and AcOH.…”

Section: Hsamentioning

confidence: 99%

Pseudo-enzymatic hydrolysis of 4-nitrophenyl acetate by human serum albumin: pH-dependence of rates of individual steps

Ascenzi

Gioia

Fanali

et al. 2012

Biochemical and Biophysical Research Communications

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Isomerization reactions of charcoal-defatted bovine plasma albumin. The N-F transition and acid expansion

Cited by 186 publications

References 40 publications

Muscle beta-actinin and serum albumin of the chicken are indistinguishable by physicochemical and immunological criteria.

Muscle beta-actinin and serum albumin of the chicken are indistinguishable by physicochemical and immunological criteria.

Conformational Transitions of the Three Recombinant Domains of Human Serum Albumin Depending on pH

Pseudo-enzymatic hydrolysis of 4-nitrophenyl acetate by human serum albumin: pH-dependence of rates of individual steps

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