-transparent.png){kind=logo}
Rabbit muscle carbonic anhydrase III, a recently discovered third isoenzyme (possibly muscle specific) of carbonic anhydrase (carbonate hydro-lyase, EC 4.2.1.1) (Register, A.M., Koester, M.K. and Noltmann, E.A. (1978) J. Biol. Chem. 253, 4143--4152) has been subjected to isoelectric focusing. When monomer samples, shown to be homogeneous by both ion-exchange and molecular sieve chromatography, were analyzed by this technique, three subspecies were produced, which were similar in amino acid composition and specific CO2 hydratase activity. In addition to having either monomer or dimer status, the subspecies differed in the extent of oxidation of their sulhydryl groups and in their isoelectric pH values (9.3, 8.8, and 8.4, respectively). Also, the presence of dithiothreitol will affect their relative concentrations. These subforms are therefore designated as pseudoisoenzymes and are considered to be neither genetically nor functionally separate enzyme species.
M K Koester, and
A M Register, and
E A Noltmann
May 1985,
The Journal of biological chemistry,
M K Koester, and
A M Register, and
E A Noltmann
May 1994,
Plant physiology,
M K Koester, and
A M Register, and
E A Noltmann
January 1984,
Annals of the New York Academy of Sciences,
M K Koester, and
A M Register, and
E A Noltmann
August 2004,
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society,
M K Koester, and
A M Register, and
E A Noltmann
October 1984,
Plant physiology,
M K Koester, and
A M Register, and
E A Noltmann
March 1994,
Journal of leukocyte biology,
M K Koester, and
A M Register, and
E A Noltmann
January 1984,
Annals of the New York Academy of Sciences,
M K Koester, and
A M Register, and
E A Noltmann
April 1989,
Archives of biochemistry and biophysics,
M K Koester, and
A M Register, and
E A Noltmann
September 1982,
The Biochemical journal,
M K Koester, and
A M Register, and
E A Noltmann
January 1963,
Annales d'histochimie,
