Molekulare Anthropologie

@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 und 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. und GOODMAN, MORRIS und TANIS, ROBERT J. und FERRELL, ROBERT E. und 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. und Goodman, Morris und Ferrell, Robert E. und Tanis, Robert J.",
    title = "Evolution der Carbonic Anhydrase bei Primaten und anderen Säugetieren",
    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. und Goodman, M. und Ferrell, R. E. und Tanis, R. J",
    title = "Evolution of Carbonic Anhydrase in Primates and Other Mammals, in Goodman, M., und 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., und Tanis, R. J., 1976, Evolution of Carbonic Anhydrase in Primates and Other Mammals, in Goodman, M., und Tashian, R. E., eds., Molecular Anthropology: New York, Plenum.}"
}

@incollection{tashian1980evolution,
    author = "Tashian, R. E. und Hewett-Emmett, D. und Stroup, S. K. und Goodman, M. und Yu, Y.-S. L.",
    title = "Evolution der Struktur und Funktion der Carbonic-Anhydrase-Isozyme bei Säugetieren",
    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"
}

Die Aktivität der Carbonic anhydrase in intakten Erythrozyten von sieben Säugetierarten wurde bei 25 Grad C, pH 7,4, durch Massenspektrometrie unter Verwendung der 18O-Austauschtechnik bestimmt. Die sieben Arten waren Cavia porcellus, Mustela putorius furo, Felis domesticus, Canis familiaris, Homo sapiens, Equus caballus und Bos taurus. Die als Funktion der Hämoglobinkonzentration (std kcat) bestimmten Carbonic anhydrase-Aktivitäten für intakte Erythrozyten bei pH 7,4 unterschieden sich für jede Art nicht signifikant von denen, die für lysierte Erythrozyten bei pH 7,20 bestimmt wurden. Die Carbonic anhydrase-Aktivität intakter Erythrozyten wurde durch eine Acetazolamid-Konzentration nicht verändert, die sie in der Lyse (10(-7) M) in den für den Assay benötigten 5-10 Minuten um 85% hemmte. Ethoxzolamid, ein weiterer Carbonic anhydrase-Inhibitor, erzeugte jedoch in Erythrozytensuspensionen innerhalb von 1-2 Minuten die gleiche fraktionale Hemmung der Enzymaktivität wie in der Lyse. Somit war die Hemmkonstante, Ki, in intakten und lysierten Zellen jeder Art ungefähr gleich, und es war möglich, die scheinbare molare Enzymkonzentration innerhalb der Erythrozyten aus der Konzentration des gebundenen Inhibitors zu messen. Die intrazellulären Enzymkonzentrationen waren bei Arten mit größeren Zellen höher, aber die spezifische Aktivität der Carbonic anhydrase pro Molekül war geringer, sodass die gesamte Enzymaktivität, std kcat, nicht mit dem mittleren Zellvolumen zusammenhing. Die effektive Permeabilität der Zellen für den Selbsttausch des Bicarbonat-Ions, P(HCO3-), betrug im Durchschnitt 2 X 10(-4) cm x s-1 und unterschied sich nicht zwischen den Arten.

@article{dodgson1983carbonic,
    author = "Dodgson, S. J. und 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. und Curtis, Peter J.",
    title = "Molekulare Evolution der Carbonicanhydrase-Gene: Berechnung der Divergenzzeit für Maus-Carbonicanhydrase I und 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 und Zhu, X.L. und Sly, W.S.",
    title = "Membran-assoziierte Carbonicanhydrase aus Rattenlungen. Reinigung, Charakterisierung, Gewebeverteilung und Vergleich mit Carbonicanhydrase IVs anderer Säugetiere.",
    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 molekulare Evolution von -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 und Tolvanen, Martti E. E. und Ortutay, Csaba und 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"
}