THE EVOLUTIONARY RELATIONSHIPS OF THE ENZYMES INVOLVED IN BLOOD COAGULATION AND HEMOSTASIS *

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/73621/1/j.1749-6632.1981.tb29759.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

N-Terminal sequence of creatine kinase from skeletal muscle of rabbit and rhesus monkey

1. 1. The first 20 amino acids from the N-terminus of skeletal muscle (MM) creatine kinase from both rabbit and rhesus monkey have been identified and these sequences show considerable homology.2. 2. Contrary to an earlier report, the N-terminus was not found to be blocked.3. 3. Both of these sequences show much less homology with the N-terminal sequence of heart muscle (MM) creatine kinase and no homology with that of the heart muscle mitochondrial (MiMi) isozyme.4. 4. No homology was found between the N-terminal sequence of the mitochondrial isozyme and the URF (unidentified reading frame) proteins of the human mitochondrial genome, indicating that the mitochondrial enzyme is encoded by nuclear genes. This suggests the possibility that an N-terminal peptide may be cleaved from the mitochondrial isozyme on its translocation across the mitochondrial membrane.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/25924/1/0000487.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

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

Red Cells Genetically Deficient in Carbonic Anhydrase II Have Elevated Levels of a Carbonic Anhydrase Indistinguishable from Muscle CA III a

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/71425/1/j.1749-6632.1984.tb12351.x.pd

Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements

The nucleotide sequence of the 5' region of the human carbonic anhydrase II gene has been determined. This sequence begins 643 base pairs upstream from the ATG start site and continues through exon 1, intron 1, exon 2 and the adjoining 125 nucleotides of intron 2. The human sequence is compared with homologous regions of the mouse (YBR strain) carbonic anhydrase II gene by aligning the two sequences for optimal homology. In addition to a TATA box and a putative CCAAT box (CCACC in human and CCACT in mouse), three conserved tandem-repeat elements in mouse and two in human (consensus: cCNGTCACCTCCgC) are located 15 and 22 base pairs upstream, respectively, from the CCAAT boxes in the human and mouse sequences. This repeat element is similar to a tandem repeat sequence located at about the same position in mammalian [beta]-globin genes, and may represent regulatory elements common to both the carbonic anhydrase and [beta]-globin genes. The regions surrounding exon 1 are extremely G + C-rich in both human and mouse genes. In addition, severel CCGCCC or GGGCGG sequences which may be important for transcriptional efficiency are found in the 5' flanking regions of the human and mouse genes.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/25466/1/0000004.pd

Amino acid substitution and chemical characterization of a Japanese variant of carbonic anhydrase I: CA I Hiroshima-1 (86 Asp → Gly)

An electrophoretic variant of red cell carbonic anhydrase I, designated CA I Hiroshima-1, has been observed in 12 apparently unrelated individuals during a survey of 13,019 individuals from the cities of Hiroshima and Nagasaki, Japan. Analyses of tryptic and chymotryptic peptide patterns of this CA I variant purified from 8 of the 12 individuals revealed the same altered peptides in each case. Examination of the amino acid sequence of an altered tryptic peptide purified from one of the variants showed that the aspartic acid residue at position 86 was replaced by a glycine residue. Thermostability studies demonstrated that all samples of CA I Hiroshima-1 were less stable than normal CA I. The specific esterase ( p -nitrophenyl acetate) activities of the normal and variant CA I isozymes were essentially the same. The difference spectra of the normal and variant enzymes were essentially the same. The isoelectric focusing patterns of CA I Hiroshima-1 showed a different pattern of minor bands to those produced by normal CA I. The relative amounts of the normal and variant enzymes purified from single heterozygous individuals were similar.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/44139/1/10528_2004_Article_BF00484625.pd