Photoaffinity labelling of the nucleoside transporter of cultured mouse lymphoma cells.

Abstract	Nitrobenzylthioniosine (NBMPR), a potent and specific inhibitor of nucleoside transport, is bound reversibly by high affinity sites on nucleoside transporter proteins of erythrocyte membranes and, upon photoactivation, NBMPR molecules become covalently bonded to the sites. This study showed that [3H]NBMPR molecules reversibly bound to intact S49 and L5178Y mouse lymphoma cells became covalently bound upon exposure to UV light. Electrophoretic analysis of plasma membrane fractions from the labelled cells showed that 3H was present in polypeptides which migrated as a major band with an apparent Mr of 45000-65000.
Authors	A F Almeida, S M Jarvis, J D Young, A R Paterson
Journal	FEBS letters (FEBS Lett) Vol. 176 Issue 2 Pg. 444-8 (Oct 29 1984) ISSN: 0014-5793 [Print] England
PMID	6489528 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Affinity Labels Blood Proteins Membrane Proteins Nucleoside Transport Proteins Thioinosine Inosine 4-nitrobenzylthioinosine
Topics	Affinity Labels (metabolism) Animals Blood Proteins (metabolism) Cell Line Electrophoresis, Polyacrylamide Gel Erythrocyte Membrane (metabolism) Inosine (analogs & derivatives) Leukemia L5178 (metabolism) Lymphoma (metabolism) Membrane Proteins (metabolism) Mice Nucleoside Transport Proteins Photochemistry Thioinosine (analogs & derivatives, metabolism) Ultraviolet Rays

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