Studies on immunological properties of enolase from carp muscles (Cyprinus carpio) after chemical modification of some amino-acid residues

After modification of histidine residues, enolase from carp muscles lost the ability to precipitate with antibodies against native enzyme. This ability remained after nitration of tyrosine residues, but the immunoelectrophoretic pattern--localisation and height of arcs--differed from that of native...

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Bibliographic Details
Published inArchivum Immunologiae et Therapiae Experimentalis Vol. 34; no. 1; p. 93
Main Authors Kustrzeba-Wójcicka, I, Pietkiewicz, J, Wolna, E
Format Journal Article
LanguageEnglish
Published Switzerland 1986
Subjects
Amino Acids - immunology
Animals
Carps - metabolism
Cyprinidae - metabolism
Epitopes - immunology
Histidine - metabolism
Immunoelectrophoresis - methods
Immunoelectrophoresis, Two-Dimensional - methods
Muscles - enzymology
Phosphopyruvate Hydratase - immunology
Protein Processing, Post-Translational
Structure-Activity Relationship
Tryptophan - metabolism
Tyrosine - metabolism
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Summary:After modification of histidine residues, enolase from carp muscles lost the ability to precipitate with antibodies against native enzyme. This ability remained after nitration of tyrosine residues, but the immunoelectrophoretic pattern--localisation and height of arcs--differed from that of native enolase. Minor changes of this pattern were found in enolase with modified tryptophan residues.
ISSN:0004-069X