Gasanalyse, Wasserstoff und Kohlenwasserstoffe

Bosshard, E.; Fischli, E.; Anderson, R.; Katz, Mikael; Lebeau, Philippe; Damiens, Audrey; Krieger, A.; Neubeck, C.; Whiton, L. C.; Reinecke, J. R.; Merriam, E. S.; Birchby, J. A.; Engelder, Carl J.; Terres, E.; Mauguin, E.; Burell, G. A.; Oberfell, H. H.; SnydamJr., J. R.; Piva, Andrea; Hofmann, K. A.; Gautier, A.; Hawley, F. G.; Richter, Erich O.; Nestel, R. J.; Anderson, Edwin; Weyl, Th.; Zeitler, Hans-Jörg; Henrich, F.; Shipley, J. W.; Thiele, Johannes; Centnerszwer,; Biedermann, W.; Riffe, J.; Watson, E.; Franzen, Hartwig; Sieverts, Ad.; Brandt, R.; Keiser, Edward H.; Master, Le Roy Mc; Usher, F. L.; Rao, Bh. S. V. Raghava; Jones, G. W.; Doherty, H. G.; Higgins, Harold L.; Marriot, W. Mc Kim; Knorre, von; Hurding, E. P.; Johnson, Einar; Bride, B. S. Mc; Edwards, J. D.; Edwards, Alfred

doi:10.1007/bf01452080

Cited by 3 publications

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“…A method for staining proteins prior to polyacrylamide gel electrophoresis with Remazol Brilliant Blue R [15] and Drimarene Brilliant Blue, [16] two reactive dyes containing an ethyl sulfone and a difluorochloropyrimidyl group, respectively, has been described. Non-fluorescent benzotria- [a] Department of Chemistry, University of Minho, Gualtar, 4710-057 Braga, Portugal Fax: (internat.)…”

Section: Introductionmentioning

confidence: 99%

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Chromophoric Azo Reagents for Amino Acid and Peptide Labelling

et al. 2004

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Section: Introductionmentioning

confidence: 99%

“…HRMS: calcd. for C16 H 19 N 5 O 3 S [M ϩ ] 361.1209; found 361.1214. The product of the reaction of 2 with isoleucine methyl ester hydrochloride (203 mg, 1.12 mmol) was chromatographed with chloroform/methanol (5.8:0.2) as the eluent to give the ester 6b (350 mg, 75%).…”

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Chromophoric Azo Reagents for Amino Acid and Peptide Labelling

et al. 2004

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“…"-labeled cytochrome c plus carrier from experiments F and B were each mixed with uniformly [14C]acetylated cytochrome c (20 nmol, 70 Ci/mol [12]). The ['4C]acetylated cytochrome c served as a concentration standard [13]. At this stage, more cytochrome c serving as a carrier was added so that in both experiments the total amount of cytochrome c was 1 pmol.…”

Section: Methodsmentioning

confidence: 99%

“…This difference in the reaction conditions led to a generally lower labeling of cytochrome L' in the presence of the antibody. The different conditions can be corrected for by inclusion of an internal standard which reacts with acetic anhydride independently of cytochrome c or antibody [13]. Such a correction was made in a previous application of this method [8], but even without such a correction we could distinguish unequivocally between less reactive atid equally reactive residues (see R,,, values in Table 1).…”

Section: Sine Rcsidi~esmentioning

confidence: 99%

“…A small amount of [3H]acetic anhydride was used for differential acetylation. The degree of 3H-labeling was typically around 0.3 mol [3H]acetyl/mol cytochrome c. A low initial degree of labeling guarantees that R is a direct reflection of the binding of the monoclonal antibody to cytochrome c. If several lysines were labeled in the initial labeling reaction, a change of chemical reactivity toward acetic anhydride could result from various changes of conformation brought about by acetylation per se [13]. Fig.…”

Section: Differential Ucetylutionmentioning

confidence: 99%

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Mapping of four discontiguous antigenic determinants on horse cytochrome c

Oertle

Immerglück

Paterson

et al. 1989

European Journal of Biochemistry

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The epitopes (antigenic determinants) recognized by four different monoclonal antibodies on horse cytochrome c have been partially characterized by differential acetylation of lysine residues of free and antibodybound cytochrome c. The degree of acetylation in the bound and free antigen molecule was assessed by a double-labeling procedure with [3H]acetic anhydride and [14C]acetic anhydride. Out of the 19 lysine residues of cytochrome c only very few were less reactive in the antigen-antibody complex, i.e. presumably located at the epitope for the antibody under study. The protection varied from 1.5-fold to over 20-fold lower reactivity in antibody-bound cytochrome c. The present results are complemented by previous data obtained by cross-reactivity analysis with cytochromes c from different species, with chemically modified cytochrome c derivatives, and by inhibition of proteolysis of cytochrome c in the presence of the antibodies. From the combined data we conclude that each of the four epitopes depends on the precise spatial folding of the antigen and contains residues which are brought together by the folding of the polypeptide chain. This work exemplifies that mapping of conformationdependent epitopes can be achieved by applying a combination of mapping procedures of which each by itself provides partial information.

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Monoclonal antibody recognizes a conformational epitope in a random coil protein

Saad

Corradin

Bosshard

1988

European Journal of Biochemistry

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The antigenic determinants for two monoclonal antibodies directed against horse apo-cytochrome c, a protein of disordered structure, as judged by spectroscopic and hydrodynamic criteria, have been studied by a combination of methods: antigen competition in solution by radio immunoassay and enzyme-linked immunoassay, and differential acetylation of free and antibody-bound antigen. In the latter method the accessibility of lysine residues of the antigen in the antigen-antibody complex is compared to the accessibility in the free antigen. The two antibodies against the heme-free protein do not recognize intact native cytochrome c, but they crossreact with the heme-containing peptides 1-38 and 1-65 of cytochrome c. The antigenic determinant recognized by monoclonal antibody SJL 2-4 is conformational and discontiguous, it is composed of residues close to the N-terminus and around position 25. The other monoclonal antibody, Cyt-1-59, seems to recognize a contiguous epitope close to the N-terminus. The present results show that even a seemingly disordered protein which is conventionally classified as a random coil may feature subtle spatial regularities. The presence of ordered conformational elements in apocytochrome c may be important for the enzyme-catalyzed covalent attachment of the heme and the import of cytochrome c into mitochondria. A discontiguous determinant for SJL 2-4 is particularly interesting because this antibody inhibits the proliferation of a T-cell clone specific for apo-cytochrome c [Corradin & Engers (1984) Nature (Lond.) 308, 547-548].

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Gasanalyse, Wasserstoff und Kohlenwasserstoffe

Cited by 3 publications

References 0 publications

Chromophoric Azo Reagents for Amino Acid and Peptide Labelling

Chromophoric Azo Reagents for Amino Acid and Peptide Labelling

Mapping of four discontiguous antigenic determinants on horse cytochrome c

Monoclonal antibody recognizes a conformational epitope in a random coil protein

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