Ca2(+)-binding site of carp parvalbumin recognized by monoclonal antibody.
Monoclonal antibody 235 which was used for immunohistochemical staining of parvalbumin in tissue sections partially protects Lys-54 of carp muscle parvalbumin from reaction with acetic anhydride in the parvalbumin-antibody complex. Lys-54 is located in the CD-loop of parvalbumin and is flanked by the Ca2(+)-ligands Asp-53 and Ser-55 of the Ca2(+)-site I. Another monoclonal antibody against carp parvalbumin, mca 239, partially protects lysine residues 27, 32, 87 and 107, indicating that this antibody is directed against a discontinuous epitope distant from the two Ca2(+)-binding sites of parvalbumin.
Biochemisches Institut, Universität Zürich, Switzerland.
R
R
Tinner
M
M
Oertle
C W
CW
Heizmann
H R
HR
Bosshard
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D002347:Carps / Q000378:metabolism*; D003530:Cyprinidae / Q000378:metabolism*; D000939:Epitopes; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000378:metabolism*; D010320:Parvalbumins / Q000276:immunology / Q000378:metabolism*; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D000939:Epitopes; D009124:Muscle Proteins; D010320:Parvalbumins; D002118:Calcium