M. Petef
Uppsala University
6 Papers
351 Citations
M. Petef is an academic researcher from Uppsala University. The author has contributed to research in topics: Carbonic anhydrase & Binding site. The author has an hindex of 6, co-authored 6 publications.
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Papers
Crystal structure of human carbonic anhydrase C.
Anders Liljas,Anders Liljas,K.K. Kannan,P.-C. Bergstén,I. Waara,K. Fridborg,B. Strandberg,U. Carlbom,L. Järup,S. Lövgren,M. Petef +10 more
TL;DR: The three dimensional structure of human carbonic anhydrase C has been determined at 2.0 A resolution and the active site has been identified by the binding of inhibitors and the location of the zinc ion.
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Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution
TL;DR: The three-dimensional structure of carbonic anhydrase B (EC 4,2,1,1; carbonate hydro-lyase) from human erythrocytes has been determined to high resolution and the tertiary structure is unique for its folding and is very similar to the structure of the isoenzymes.
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Crystal structure of human erythrocyte carbonic anhydrase C. VI. The three-dimensional structure at high resolution in relation to other mammalian carbonic anhydrases.
K.K. Kannan,Anders Liljas,I. Waara,P.-C. Bergstén,S. Lövgren,B. Strandberg,Bengtsson U,U. Carlbom,K. Fridborg,L. Järup,M. Petef +10 more
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Structure of human carbonic anhydrase B. I. Crystallization and heavy atom modifications.
K.K. Kannan,K. Fridborg,P.-C. Bergstén,Anders Liljas,S. Lövgren,M. Petef,B. Strandberg,I. Waara,L. Adler,S.O. Falkbring,P.O. Göthe,P.O. Nyman +11 more
TL;DR: Human carbonic anhydrase B has been crystallized from 2.3 m -ammonium sulphate solution at pH 8.7 using a method for reproducible crystallization and the position of the essential zinc ion has been established from two projections.
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Structure and function of carbonic anhydrase: comparative studies of sulphonamide binding to human erythrocyte carbonic anhydrases B and C
K.K. Kannan,I. Vaara,B. Notstrand,S. Lövgren,A. Boren,K. Fridborg,M. Petef +6 more
- 01 Jan 1977
TL;DR: Soon after the discovery of carbonic anhydrase from bovine erythrocytes, it was shown that aromatic and heterocyclic sulphonamides with unsubstituted R—SO2 NH2 groups constitute a class of powerful inhibitors, while aliphatic sulph onamides are poor inhibitors of the carbonicAnhydrases.
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