GENETIC AND PHYLOGENETIC VARIATION IN THE DIFFERENT MOLECULAR FORMS OF MAMMALIAN ERYTHROCYTE CARBONIC ANHYDRASES *

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/73183/1/j.1749-6632.1968.tb11878.x.pd

Isoenzymes of carbonic anhydrase I from primate red blood cells

The electrophoretic patterns of the multiple forms of carbonic anhydrase I were examined from the red cells of two species of macaque monkeys and orangutan. In the rhesus macaque, Macaca mulatta, it was possible to generate both anodal and cathodal electrophoretic components when a single component was isolated and electrophoresed again. These findings suggest that the alternate forms of carbonic anhydrase I are conformational isoenzymes rather than the result of such processes as binding, deamination, and proteolytic action.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/33668/1/0000178.pd

Genetic variation in the carbonic anhydrase isozymes of macaque monkeys. I. The radioimmunosorbent assay

A radioimmunosorbent technique is described which is capable of independently detecting both isozymes of carbonic anhydrase, CA I and CA II, in concentrations as low as 1 ng/ml. The technique is used to quantitate the different electrophoretic variants of red cell CA I as well as levels of CA II in the pig-tailed macaque, Macaca nemestrina .Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/44181/1/10528_2004_Article_BF00485543.pd

The Value of Inherited Deficiencies of Human Carbonic Anhydrase Isozymes in Understanding Their Cellular Roles a

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/73265/1/j.1749-6632.1984.tb12346.x.pd

Organization of the Mouse and Human Carbonic Anhydrase II Genes a

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/75491/1/j.1749-6632.1984.tb12355.x.pd

Absence or Reduction of Carbonic Anhydrase II in the Red Cells of the Beluga Whale and Llama: Implications for Adaptation to Hypoxia

Carbonic anhydrase (CA) expression was examined in the red cells of two mammals that have adapted to low oxygen stress: the llama, which has adapted to high altitudes, and the beluga (or white) whale, which routinely dives for extended periods. Immunodiffusion analyses of their Hb-free hemolysates and partial amino acid sequencing of their HPLC-separated nonheme proteins indicate that the low-activity CA I isozyme is the major nonheme protein in erythrocytes of both the beluga whale and the llama. The high-activity CA II isozyme was not detected in the whale red cells but was present at low levels in erythrocytes of the llama. These results suggest that the absence or decrease in the expression of the high-activity CA II isozyme may be advantageous under hypoxic conditions.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/44163/1/10528_2004_Article_226852.pd

Enzymatic synthesis of carbonic anhydrases by human reticulocytes

Human reticulocyte-rich blood incubated 4h at 37[deg] in O2-CO2 (95:5, v/v) with 3H- or 14C-tagged amino acids revealed incorporation of the label into carbonic anhydrase I and II, Hb A, and in one patient, into Hb S. No radioactivity could be detected in normal, nonreticulocyte-rich blood similarly treated. From this, it is concluded that the anucleate human reticulocyte synthesizes carbonic anhydrase I and II by means of a stable messenger RNA in the absence of DNA.During the course of this study, several new methods were developed for the microanalysis of proteins including (1) comparison of labeled protein components after electrophoresis by liquid scintillation counting of consecutive slices of starch gels with autoradiography, (2) isolation of 1-mg quantities of carbonic anhydrase from whole blood hemolysates followed by tryptic digestion and fingerprinting of 0.01 mg samples on thin-layer chromatography support sheets, and (3) autoradiographs of the fingerprints by apposition to AR10 film plates and recording the film reduction by light microscopy and photomicrography.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/32866/1/0000244.pd

Genetic variation in the carbonic anhydrase isozymes of macaque monkeys : III. Biosynthesis of carbonic anhydrases in bone marrow erythroid cells and peripheral blood reticulocytes of Macaco nemestrina

The carbonic anhydrase isozymes (CA I and CA II) of the pig-tailed macaque, Macaca nemestrina, have been chosen to study the regulation of enzyme levels in red blood cells. Two quantitative variants of CA I that are ideal for studies of enzyme regulation exist in this species. One variant is one of four known electrophoretic types of CA I, designated CA Ia, which is present at levels about 30% of those of the other electrophoretic types. The other is a deficiency variant of CA I which, in homozygotes, reduces the product of the CA I locus about 5000-fold and reduces the product of the CA II locus by about 60%. -[14C]Serine was used to study the biosynthesis of CA I and CA II isozymes in the reticulocytes of animals carrying these CA I variants. Specific radioactivity and total incorporation data from bone marrow erythroid cells, and peripheral blood reticulocytes indicate that the reduced CA Ia concentration is probably the result of degradation. This degradation appears to occur for only a short time before the reticulocytes enter the peripheral blood. It was not possible to determine whether the 5000-fold reduction of CA I in the CA I-deficient animals is due to reduced transcription, reduced translation, or degradation. The effect of the CA I-deficiency mutation on the synthesis of CA II was also studied. For each dose of CA I-deficiency gene, there appears to be a 30% reduction in the rate of -[14C]serine incorporation into CA II, thereby accounting for the reduced CA II concentration in CA I-deficient animals.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/33820/1/0000077.pd

Unexpected expression of carbonic anhydrase I and selenium‐binding protein as the only major non‐heme proteins in erythrocytes of the subterranean mole rat (Spalax ehrenbergi)

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/117190/1/feb2s0014579398006905.pd

Characterization of a new variant of human red cell carbonic anhydrase I, CA if London (Glu-102→Lys)

A new inherited variant of red cell carbonic anhydrase I (CA I), designated CA If London, was discovered during a survey of 1615 individuals from London, England. No electrophoretic variants of the other isozyme of carbonic anhydrase CA II, were observed in the same survey. Sequence analysis of a lysine-blocked tryptic peptide believed to contain the amino acid substitution in CA If showed that the glutamyl residue at position 102 had been substituted by a lysyl residue. This substitution results in a net increase of two positive charges in the mutant enzyme. Densitometric scanning of the electrophoretically separated forms in the variant hemolysate indicates that the levels of the normal and variant enzymes are approximately equal.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/44118/1/10528_2004_Article_BF00485993.pd