Binding sites of photoreceptor-specific antibodies COS-1, OS-2 and AO
作者:
RöhlichPÁL,
SzélÁgoston,
期刊:
Current Eye Research
(Taylor Available online 1993)
卷期:
Volume 12,
issue 10
页码: 935-944
ISSN:0271-3683
年代: 1993
DOI:10.3109/02713689309020400
出版商: Taylor&Francis
数据来源: Taylor
摘要:
The chicken red-sensitive cone visual pigment iodosin) and several synthetic peptides of cone and rod tisuar pigments were used to find the binding sites of our photoreceptor-specific antibodies with immunocytochemistry. The ability of iodopsin to block immunolabeling with monoclonal antibodies COS-1 and OS-2 furnished direct evidence that both antibodies are specific to visual pigments. lmmunocytochemistry on whole-mount retinas with and without detergent, as well as electron microscopic labeling of cone photoreceptor membranes revealed the binding sites of COS-1 and OS-2 to be on the cytoplasmic side of the membrane. By testing several synthetic peptides, mainly from the C-terminal region of the cone visual pigments, we found that the domain consisting of the last 6 amino acids of the human red/green-, and the chicken red-sensitive cone pigments completely blocked immunolabeling with COS-1, while the sequence consisting of the last 12 amino acids of the human blue cone pigment was effective to block the binding of OS-2. Both monoclonals can be regarded therefore C-terminal specific antibodies. OS-2 was found to bind to the dark-adapted photopigment more strongly than to the light-adapted one. The binding of the polyclonal rhodopsin antibody AO was almost entirely inhibited by the N-terminal synthetic peptide of bovine rhodopsin indicating that this antibody binds primarily to the N-terminal domain of rhodopsin in a tissue environment.
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