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When human serum albumin (HSA) is added to rat liver microsomes, the formation of carbon monoxide from [14C]heme  becomes a time-dependent process that is inhibited in a concentration-dependent manner by 8-anilino-1-naphthalene sulfonic acid. This inhibition is specific for carbon monoxide formation, as shown by the fact that heme breakdown to biliverdin, protoporphyrin IX, or iron is not affected by the inhibitor. These results indicate that the effect of HSA is mediated by the induction of heme oxygenase activity. In order to further define the conditions under which heme oxygenase activity may be induced, the effects of the addition of various classes of proteins or selected amino acids to the microsomal incubation mixture were investigated. Incubation of HSA with microsomes at either 20 degrees C or 37 degrees C for 5 min did not affect heme oxygenase activity; however, 30-min preincubation of the microsomes with 50 microM HSA was needed to inhibit the activity of the enzyme. The heme oxygenase inhibitor, tin mesoporphyrin, did not reverse the inhibition of heme oxygenase activity by HSA. HSA inhibited heme oxygenase activity when added to the reaction mixtures at concentrations up to 1 microM. With higher concentrations, HSA was found to inhibit carbon monoxide formation, but the enzyme was still inactivated by the addition of as little as 0b46394aab