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Distinctive Properties or the Purified Na‐Ca Exchanger from Rod Outer Segments a
Author(s) -
LESER GEORGE P.,
NICOLL DEBORA A.,
APPLEBURY MEREDITHE L.
Publication year - 1991
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1991.tb17309.x
Subject(s) - physics , chemistry
The Na-Ca exchanger of rod outer segments plays an important role in the regulation of Ca levels in photoreceptor cells. While this transporter shares functional properties with other Na-Ca exchangers, it has several unique features. The purified ROS exchanger migrates as a single band at 220 kDa in SDS-polyacrylamide gels, indicating that the unit size of its polypeptide is larger than other known Na-Ca exchangers (and most transporters). A specific antiserum to the ROS exchanger does not bind to the Na-Ca exchangers found in sarcolemmal vesicles or brain synaptic plasma membranes. Similarly, polyclonal antiserum specific for the cardiac exchanger does not react with ROS or brain proteins. The ROS exchanger requires K for transport activity. By incorporating the purified exchanger into proteoliposomes and measuring the sequestration of K, the actual transport of K is demonstrated. A stoichiometry of 4Na:1Ca,1K for the exchanger of ROS has been measured.