ABSTRACT
PURPOSE: To determine the response rate of patients with refractory/relapsed non-Hodgkin's lymphoma to treatment with elsamitrucin and to further characterize the toxic effects of elsamitrucin in this group of patients. PATIENTS AND METHODS: Eligibility required pathologically verified relapsed or refractory non-Hodgkin's lymphoma with no more than two prior chemotherapy regimens for patients with tumors classified by the International Working Formulation (IWF) as A-C and no more than one prior chemotherapy for those with IWF grades D-G. Patients were entered with either normal or impaired bone marrow function, but normal liver function tests were required unless clearly related to lymphomatous involvement of the liver. Elsamitrucin 25 mg/m2 was administered intravenously over 5-10 minutes weekly. RESULTS: Thirty-one patients entered the study and were treated for a median of six weeks (range 1-42). All patients were evaluable for toxicity and 30 for response. Mild nausea and/or vomiting and asthenia were the most frequently reported adverse events. Four (13%, 95% Cl 4.4-31.6%) partial responses were seen along with two (7%) minor responses while 9 (30%) patients had stable disease. CONCLUSION: Elsamitrucin showed modest activity in patients with relapsed or refractory non-Hodgkin's lymphoma. Toxicity was relatively mild, consisted mainly of asthenia, nausea and vomiting and did not include myelosuppression. The activity of elsamitrucin in this group of patients and its lack of myelosuppression suggest utility in this disease especially when combined with other proven agents.
Subject(s)
Aminoglycosides , Anti-Bacterial Agents/therapeutic use , Antibiotics, Antineoplastic/therapeutic use , Lymphoma, Non-Hodgkin/drug therapy , Adult , Aged , Aged, 80 and over , Anti-Bacterial Agents/adverse effects , Antibiotics, Antineoplastic/adverse effects , Female , Humans , Male , Middle AgedABSTRACT
A new method is described for purification of the dehydropeptidase I enzyme, renal dipeptidase (EC 3.4.13.11). The six steps used are homogenization of the tissue, extraction with Triton X-100, sedimentation of insoluble material, and ion-exchange, size-exclusion, and affinity chromatographies. The use of Triton X-100 to solubilize the enzyme is a major advantage over the previously described procedure using n-butanol and results in both improvements in yield and interexperimental consistency. Also, the affinity column method we have employed results in higher recovery of active enzyme at the final step and a product which is apparently homogeneous. The method has general utility for this class of enzymes.
