1986 Fiscal Year Final Research Report Summary

Clinical and Basic Study on Human Erythrocyte Carbonic Anhydrase I-Presence of a Mixed Disulfide with Glutathione.

Research Project

Project/Area Number	60570547
Research Category	Grant-in-Aid for General Scientific Research (C)
Allocation Type	Single-year Grants
Research Field	Hematology
Research Institution	Hokkaido University
Principal Investigator	KONDO Takahito Hokkaido University School of Medicine, Instructor, 医学部, 助手 (00158908)
Project Period (FY)	1985 – 1986
Keywords	Erythrocyte / Carbonic anhydrase I / Primary aldosteronism / グルタチオン
Research Abstract	A low activity form of carbonic anhydrase I was found in erythrocytes of five patients with primary aldosteronism. The specific activity was very low, however the activity was restored by drug treatment as well as adrenalectomy. The enzyme was purified to homogeneity from one of the patients. The enzyme was not distinguishable with respect to its antigenecity and zinc content. On theother hand, the inhibition constant and binding affinity to a specific inhibito, acetazolamide, was quite different. Sulfhydryl titration, amino acid analysis and peptide mapping analysis suggested that the low activity from contains a mixed disulfide with glutathione which is closely associated with its low activity form. This result supports our previous findings on <gamma> -glutamyl cyclotransferase and N-acetyl hexosaminidase, both of which were found to contain a mixed disulfide with glutathione. The presence of a mixed disulfide in the protein seems to be a common phenomenon.