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By George Weber (auth.), Joseph G. Cory, Andor Szentivanyi (eds.)

In anticipation of the outlet of the H. Lee Moffitt melanoma middle and examine lnstitut~ at the campus of the collage of South Florida, a global symposium, "The First Annual H. Lee Moffitt Symposium on melanoma Biology and Therapeutics" used to be held in Tampa, Florida on January 20-22, 1986. during this first symposium we determined to give a broad-based sequence of themes facing the most important concerns within the box of melanoma. those issues ranged from the biochemistry of the melanoma cellphone to the layout of antineoplastic brokers, via tumor telephone heterogeneity, remedy of ltuman neoplasms to immunological facets of melanoma biology and tr~atment. The audio system selected represented members of foreign acclaim who're very energetic within the sector of melanoma learn and remedy. The symposium introduced jointly scien­ tists/physicians from six countries together with Austria, Canada, France, Hungary, West Germany, and naturally, the USA. The congeniality of the members promoted the pleasant trade of data which, it really is was hoping, will enormously hasten the time whilst winning administration of human melanoma becomes regimen. destiny symposia during this sequence may be hugely centred and may care for a unmarried side of this huge box of melanoma learn and remedy. Joseph G. Cory, Editor Andor Szentivanyi, Editor collage of South Florida, 1986 V ACKNOWLEDGMENTS This quantity provides the complaints of the H. Lee Moffitt foreign Syn~osium on melanoma Biology and Therapeutics which was once held in Tampa, Florida on January 20, 21, and 22, 1986.

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The activity of F-ara-A caused us to study other haloadenine nucleosides. -2 Table 4. 3 4 aAdenosine deaminase, V relative to adenosine at 100. bDeoxycytidine max c kinase, V re~ative co deoxyadenosine at 100. -2 cells exposed to drug for TBß. The concentration required to inhibit cell growth to 50% of controls. 28 Table 5. -2 Ic 50 (lJM) L1210a IC 50 (lJM) X y Cl Cl >120c >120c Cl Br )ll0c )ll0c Cl I )100c )100c Cl >120c >120c Cl N3 NH 2 >120d 80 F Cl 60 100 29 F N3 NH 2 100 120 12 F OH 3 9 F aCell proliferation assay (48 hr).

8 Polyacrylamide gel electrophoresis of L. casei dihydrofolate reductase complexed with NADPH and fluorescein-MTX. A, Protein stain; B, Unstained gel photographed under ultraviolet light. From (19). Dihydrofolate reductase has the unique ability to form stable substrate and inhibitor complexes. Figure 10 demonstrates the changes in electrophoretic mobility that occur when the L1210 enzyme forms binary complexes with dihydrofolate, MTX, or NADPH, and a ternary complex containing MTX and NADPH. The increased mobility that occurs when NADPH is complexed is considerably greater than can be accounted for by the additional charges introduced by the nucleotide.

Shealy, Alkaline Elution Studies of the Effect of SR! 6155, a New Chloroethylating Agent, on Cultured L1210 Cells Using Chlorozotocin and a Reference Compound, Proc. Am. Assoc. Cancer Res. 24:244 (1983). N. w. Gibson,~Plowman, L. C. Erickson, and K. Kohn, Differential Cytotoxicity and DNA Crosslinking in Normal and Transformed Human Cells Exposed to 2-Chloroethyl Methylsulfonylmethanesulfonate (NSC-334947), Proc. Am. Assoc. Cancer Res. 25:289 (1984). J. A. Alexander, B. J. Bowdon, G. P. Wheeler, and Y.

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