Active sites of the cyclic GMP phosphodiesterase gamma-subunit of retinal rod outer segments.
Monoclonal antibodies were prepared to the gamma-subunit of the cGMP phosphodiesterase. One of them gamma p-1, suppresses the activation of phosphodiesterase through the alpha-subunit of transducin. The gamma-subunit fragment 24-45 rich in Arg and Lys residues is involved in gamma p-1 binding and is essential for the gamma-subunit interaction with transducin. Carboxypeptidase Y cleaves off seven amino acid residues from the C-terminus of the gamma-subunit resulting in phosphodiesterase activation. Thus, the C-terminal fragment of gamma-subunit participates in phosphodiesterase inhibition.
Lipkin
V M
VM
Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Moscow.
Dumler
I L
IL
Muradov
K G
KG
Artemyev
N O
NO
Etingof
R N
RN
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000276:immunology / Q000378:metabolism*; D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D002417:Cattle; D000939:Epitopes / Q000032:analysis; D007700:Kinetics; D046911:Macromolecular Substances; D010786:Photoreceptor Cells / Q000201:enzymology*; D012374:Rod Cell Outer Segment / Q000201:enzymology*
D000911:Antibodies, Monoclonal; D000939:Epitopes; D046911:Macromolecular Substances; D015106:3',5'-Cyclic-GMP Phosphodiesterases