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European journal of biochemistry1969; 11(2); 267-277; doi: 10.1111/j.1432-1033.1969.tb00769.x

[Covalent structure of horse myoglobin].

Abstract: No abstract available
Publication Date: 1969-12-01 PubMed ID: 4902609DOI: 10.1111/j.1432-1033.1969.tb00769.xGoogle Scholar: Lookup
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  • Journal Article

Cite This Article

APA
Dautrevaux M, Boulanger Y, Han K, Biserte G. (1969). [Covalent structure of horse myoglobin]. Eur J Biochem, 11(2), 267-277. https://doi.org/10.1111/j.1432-1033.1969.tb00769.x

Publication

ISSN: 0014-2956
NlmUniqueID: 0107600
Country: England
Language: fre
Volume: 11
Issue: 2
Pages: 267-277

Researcher Affiliations

Dautrevaux, M
    Boulanger, Y
      Han, K
        Biserte, G

          MeSH Terms

          • Amino Acid Sequence
          • Amino Acids / analysis
          • Animals
          • Bromine
          • Carboxypeptidases
          • Cetacea
          • Chromatography, Ion Exchange
          • Chromatography, Paper
          • Chymotrypsin
          • Cyanides
          • Genetic Code
          • Globins / analysis
          • Horses
          • Myoglobin / analysis
          • Pepsin A
          • Peptides / analysis
          • Species Specificity

          Citations

          This article has been cited 9 times.
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          2. Schwarz W, Tiedemann H, Tiedemann H. High performance gel permeation chromatography of proteins. Application to embryonic inducing factors.. Mol Biol Rep 1981 Nov 30;8(1):7-10.
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          4. Twining SS, Lehmann H, Atassi MZ. The antibody response to myoglobin is independent of the immunized species. Analysis in terms of replacements in the antigenic sites and in environmental residues of the cross-reactions of fifteen myoglobins with sperm-whale myoglobin antisera raised in different species.. Biochem J 1980 Dec 1;191(3):681-97.
            doi: 10.1042/bj1910681pubmed: 6169338google scholar: lookup
          5. Tentori L. Myoglobin, with particular reference to the myoglobin of Aplysia.. Biochem J 1970 Oct;119(5):33P-34P.
            doi: 10.1042/bj1190033ppubmed: 5492807google scholar: lookup
          6. Goodman M, Moore GW, Barnabas J, Matsuda G. The phylogeny of human globin genes investigated by the maximum parsimony method.. J Mol Evol 1974 Feb 28;3(1):1-48.
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          7. Abaza MS, Atassi MZ. Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 145-151 (antigenic site 5) of myoglobin.. J Protein Chem 1992 Dec;11(6):687-98.
            doi: 10.1007/BF01024970pubmed: 1466763google scholar: lookup
          8. Abaza MS, Atassi MZ. Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 56-62 (antigenic site 2) of myoglobin.. J Protein Chem 1992 Oct;11(5):455-65.
            doi: 10.1007/BF01025022pubmed: 1280438google scholar: lookup
          9. Abaza MS, Young CR, Atassi MZ. Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 15-22 (antigenic site 1) of myoglobin.. J Protein Chem 1992 Oct;11(5):445-54.
            doi: 10.1007/BF01025021pubmed: 1280437google scholar: lookup