@article{davenport1946carbonic,
    author = "Davenport, Horace W.",
    title = "CARBONIC ANHYDRASE IN TISSUES OTHER THAN BLOOD",
    year = "1946",
    journal = "Physiological Reviews",
    url = "https://doi.org/10.1152/physrev.1946.26.4.560",
    doi = "10.1152/physrev.1946.26.4.560",
    number = "4",
    pages = "560-573",
    volume = "26"
}

@article{larimer1960a,
    author = "Larimer, J.L and Schmidt-Nielsen, K",
    title = "A comparison of blood carbonic anhydrase of various mammals",
    year = "1960",
    journal = "Comparative Biochemistry and Physiology",
    url = "https://doi.org/10.1016/0010-406x(60)90004-9",
    doi = "10.1016/0010-406x(60)90004-9",
    number = "1",
    pages = "19-23",
    volume = "1"
}

@incollection{tashian1975evolution,
    author = "TASHIAN, RICHARD E. and GOODMAN, MORRIS and TANIS, ROBERT J. and FERRELL, ROBERT E. and OSBORNE, WILLIAM R.A.",
    title = "EVOLUTION OF THE CARBONIC ANHYDRASE ISOZYMES",
    year = "1975",
    booktitle = "Isozymes",
    url = "https://doi.org/10.1016/b978-0-12-472704-5.50019-7",
    doi = "10.1016/b978-0-12-472704-5.50019-7",
    pages = "207-223"
}

@incollection{tashian1976evolution,
    author = "Tashian, Richard E. and Goodman, Morris and Ferrell, Robert E. and Tanis, Robert J.",
    title = "Evolution of Carbonic Anhydrase in Primates and Other Mammals",
    year = "1976",
    booktitle = "Molecular Anthropology",
    url = "https://doi.org/10.1007/978-1-4615-8783-5\_16",
    doi = "10.1007/978-1-4615-8783-5\_16",
    pages = "301-319"
}

@misc{tashian1976evolution1,
    author = "Tashian, R. E. and Goodman, M. and Ferrell, R. E. and Tanis, R. J",
    title = "Evolution of Carbonic Anhydrase in Primates and Other Mammals, in Goodman, M., and Tashian, R. E., eds., Molecular Anthropology",
    year = "1976",
    howpublished = "New York, Plenum",
    note = "talkorigins\_source = {true}; raw\_reference = {Tashian, R. E., Goodman, M., Ferrell, R. E., and Tanis, R. J., 1976, Evolution of Carbonic Anhydrase in Primates and Other Mammals, in Goodman, M., and Tashian, R. E., eds., Molecular Anthropology: New York, Plenum.}"
}

@incollection{tashian1980evolution,
    author = "Tashian, R. E. and Hewett-Emmett, D. and Stroup, S. K. and Goodman, M. and Yu, Y.-S. L.",
    title = "Evolution of Structure and Function in the Carbonic Anhydrase Isozymes of Mammals",
    year = "1980",
    booktitle = "Proceedings in Life Sciences",
    url = "https://doi.org/10.1007/978-3-642-67572-0\_18",
    doi = "10.1007/978-3-642-67572-0\_18",
    pages = "165-176"
}

@article{dodgson1983carbonic,
    author = "Dodgson, S. J. and Forster, R. E.",
    title = "Carbonic anhydrase activity of intact erythrocytes from seven mammals",
    year = "1983",
    journal = "Journal of Applied Physiology",
    abstract = "Carbonic anhydrase activity of intact erythrocytes from seven mammalian species was determined at 25 degrees C, pH 7.4, by mass spectrometry using the 18O-exchange technique. The seven species were Cavia porcellus, Mustela putorius furo, Felis domesticus, Canis familiaris, Homo sapiens, Equus caballus, and Bos taurus. Carbonic anhydrase activities determined as a function of hemoglobin concentration (std kcat) for intact erythrocytes at pH 7.4 were not significantly different from those determined for lysed erythrocytes at pH 7.20 for each species. The carbonic anhydrase activity of intact erythrocytes was not changed by a concentration of acetazolamide that inhibited it 85\% in lysate (10(-7) M) in the 5-10 min needed for the assay. However, ethoxzolamide, another carbonic anhydrase inhibitor, produced the same fractional inhibition of enzyme activity in erythrocyte suspensions as in lysate in 1-2 min. Thus the inhibition constant, Ki, was approximately the same in both intact and lysed cells from each species, and it was possible to measure the apparent molar enzyme concentration inside the erythrocytes from the concentration of bound inhibitor. Intracellular enzyme concentrations were greater in those species with larger cells, but the specific activity of the carbonic anhydrase per molecule was less so that the overall enzyme activity, std kcat, was not related to mean cell volume. The effective permeability of the cells to the self-exchange of bicarbonate ion, P(HCO3-), averaged 2 X 10(-4) cm x s-1 and did not vary among the species.",
    url = "https://doi.org/10.1152/jappl.1983.55.4.1292",
    doi = "10.1152/jappl.1983.55.4.1292",
    number = "4",
    pages = "1292-1298",
    volume = "55"
}

@article{fraser1986molecular,
    author = "Fraser, Peter J. and Curtis, Peter J.",
    title = "Molecular evolution of the carbonic anhydrase genes: Calculation of divergence time for mouse carbonic anhydrase I and II",
    year = "1986",
    journal = "Journal of Molecular Evolution",
    url = "https://doi.org/10.1007/bf02100637",
    doi = "10.1007/bf02100637",
    number = "4",
    pages = "294-299",
    volume = "23"
}

@article{waheed1992membraneassociated,
    author = "Waheed, A and Zhu, X.L. and Sly, W.S.",
    title = "Membrane-associated carbonic anhydrase from rat lung. Purification, characterization, tissue distribution, and comparison with carbonic anhydrase IVs of other mammals.",
    year = "1992",
    journal = "Journal of Biological Chemistry",
    url = "https://doi.org/10.1016/s0021-9258(19)50732-3",
    doi = "10.1016/s0021-9258(19)50732-3",
    number = "5",
    pages = "3308-3311",
    volume = "267"
}

@article{ludwig2011the,
    author = "Ludwig, M.",
    title = "The molecular evolution of -carbonic anhydrase in Flaveria",
    year = "2011",
    journal = "Journal of Experimental Botany",
    url = "https://doi.org/10.1093/jxb/err071",
    doi = "10.1093/jxb/err071",
    number = "9",
    pages = "3071-3081",
    volume = "62"
}

@incollection{aspatwar2014carbonic,
    author = "Aspatwar, Ashok and Tolvanen, Martti E. E. and Ortutay, Csaba and Parkkila, Seppo",
    title = "Carbonic Anhydrase Related Proteins: Molecular Biology and Evolution",
    year = "2014",
    booktitle = "Subcellular Biochemistry",
    url = "https://doi.org/10.1007/978-94-007-7359-2\_8",
    doi = "10.1007/978-94-007-7359-2\_8",
    pages = "135-156"
}