INVITRO INTERACTION OF MITOMYCIN-C AND STREPTOMYCIN-A WITH COLLAGEN

Mitomycin C and streptomycin A were studied for their interaction with soluble collagens from sepia, fish and rat skins using UV absorption spectroscopy at pH 7.4 and 3.0 and equilibrium dialysis. Both the drugs bound to collagen as shown from association constants and could be quantitatively recovered by prolonged dialysis against water showing formation of dissociable bonds between drug and collagen. At pH 7.4, mitomycin C showed greater binding affinity than streptomycin A with collagen from all three species. The reverse trend was seen at pH 3.0. Binding capacity of sepia and fish skin collagens for streptomycin A at pH 3.0 was found to be significantly greater than for mitomycin C.