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PubMed1982

Phase II study of Baker's antifol (triazinate, TZT, NSC-139,105) in advanced squamous cell carcinoma of cervix.

Thirty-two evaluable patients with advanced cervical squamous cell carcinoma were treated with Baker's antifol in a phase II study by the Gynecologic Oncology Group (GOG). There were no complete responses and five partial responses for a response rate of 15.6%. Twenty patients remained stable during the course of therapy; seven had progressive disease. The median number of courses to response was four and the median duration of response was 3 months. The dose-limiting toxicity was dermatitis, which occurred in 10 patients. In four, dermatitis was severe with ulceration and/or desquamation. In two, dermatitis was life threatening and may have contributed to death. Half of the patients had mild or moderate GI side effects; in one case it was severe. Very little hematologic toxicity was observed. No cases of respiratory depression or arrest occurred with this regimen. Baker's antifol has some activity against cervical carcinoma and may be of interest for inclusion in studies of combination therapy because of its relative lack of myelotoxicity.

Adult↗
PubMed1982

Affinity labelling of enzymes with triazine dyes. Isolation of a peptide in the catalytic domain of horse-liver alcohol dehydrogenase using Procion blue MX-R as a structural probe.

Horse liver alcohol dehydrogenase is irreversibly inactivated by Procion blue MX-R, a dichlorotriazinyl structural analogue of Cibacron blue F3G-A, with over 90% loss of activity within 30 min at pH 8.5 and 37 degrees C at a reactive dye concentration of 1 mM and enzyme subunit concentration of 5 microM. Methoxylated Procion blue MX-R does not inactivate the enzyme. The inactivation of horse liver alcohol dehydrogenase by Procion blue MX-R is competitively inhibited by the pyridine nucleotides NAD+ and NADH. Quantitatively inhibited horse liver alcohol dehydrogenase contains 1 mol dye/mol subunit of Mr 40 000. Chymotryptic digestion and resolution of the peptides by reverse-phase high-performance liquid chromatography yields a single blue peptide which on sequencing and analysis yields an amino acid sequence of: (formula; see text) with the affinity label, Procion blue MX-R, unambiguously identified as being attached to the thiol side chain of Cys-174 in the catalytic domain of the enzyme. The specific active-site-directed reaction of Procion blue MX-R with horse liver alcohol dehydrogenase is interpreted in terms of the known crystallographic structure of the enzyme.

Affinity Labels↗