Differentiation of Cl-/Ca2+-dependent and sodium dependent 3H-glutamate binding to cortical membranes from rat brain by high energy radiation inactivation analysis.
The molecular weights of 3H-L-glutamate binding in the presence of chloride and calcium ions and in the presence of sodium ions were determined by the high energy irradiation technique. The molecular weight of sodium dependent 3H-L-glutamate binding, which has pharmacological specificities similar to the high-affinity uptake system for L-glutamate, was 670,000 daltons. The high-energy radiation inactivation study of chloride and calcium dependent and sodium independent 3H-L-glutamate binding is consonant with the idea that, this binding represent glutamate transport into resealed plasma membrane vesicles.
Honoré
T
T
Drejer
J
J
Nielsen
M
M
Braestrup
C
C
D000818:Animals; D001665:Binding Sites; D001693:Biological Transport, Active / Q000528:radiation effects; D002118:Calcium / Q000494:pharmacology; D002462:Cell Membrane / Q000378:metabolism; D002540:Cerebral Cortex / Q000187:drug effects / Q000378:metabolism* / Q000528:radiation effects; D002712:Chlorides / Q000494:pharmacology; D004583:Electrons; D005971:Glutamates / Q000378:metabolism*; D018698:Glutamic Acid; D066298:In Vitro Techniques; D008970:Molecular Weight; D051381:Rats; D012964:Sodium / Q000494:pharmacology
D002712:Chlorides; D005971:Glutamates; D018698:Glutamic Acid; D012964:Sodium; D002118:Calcium