Rhodopsin kinase: two mAbs binding near the carboxyl terminus cause time-dependent inactivation.
Two mAbs generated against rhodopsin kinase (RK) were characterized for their epitopes. Both antibodies recognize short peptide sequences, overlapping but distinct, close to the carboxyl terminus. Binding of RK to the antibodies is slow. Attempts were made to use the antibodies immobilized on protein A-Sepharose beads to bind and purify the enzyme. Time-dependent inactivation of the enzyme occurred after its binding to the antibodies. Studies using different conditions to maintain the enzyme in the active form during binding or to reactivate the purified inactivated enzyme were unsuccessful.
Bruel
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Departments of Biology and Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Cha
K
K
Niu
L
L
Reeves
P J
PJ
Khorana
H G
HG
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D001666:Binding Sites, Antibody; D015153:Blotting, Western; D019556:COS Cells; D005136:Eye Proteins; D051606:G-Protein-Coupled Receptor Kinase 1; D008969:Molecular Sequence Data; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000737:chemistry / Q000276:immunology
D000911:Antibodies, Monoclonal; D005136:Eye Proteins; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases; D051606:G-Protein-Coupled Receptor Kinase 1