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  • AE1 or band 3  (1)
  • CA carbonic anhydrase  (1)
  • GTC-AP guanidium isothiocyanate-acid phenol  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 170 (2000), S. 497-504 
    ISSN: 1432-136X
    Keywords: Key words Anion exchange ; AE1 ; Red blood cells ; Lamprey ; Respiration ; AbbreviationsA carbonic anhydrase activity ; CA carbonic anhydrase ; DIDS 4,4′ diisothiocyanatostilbene-2,2′ disulphonic acid ; GTC-AP guanidium isothiocyanate-acid phenol ; IgGs type G immunoglobins ; P red blood cell HCO−3 permeability ; PCR polymerase chain reaction ; rbc(s) red blood cell(s)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The purpose of the present study was to examine the distribution of the anion exchange protein in the sea lamprey. Southern blots showed that genomic DNA of juvenile lampreys possesses several regions that are similar to segments of the AE gene from other vertebrates. However, physiological experiments examining rapid anion fluxes across the red blood cell (rbc) membrane and molecular experiments examining mRNA transcript levels both indicated that the anion exchange protein is absent in sea lamprey rbcs. In contrast, lamprey kidney, skeletal muscle, liver and heart tissue all appeared to possess mRNA transcripts for an AE protein. Further evidence for the presence of an AE protein in kidney tissue was obtained from Western blots. In order to evaluate the impact of the apparent rbc anion exchange limitations, the bicarbonate permeability of lamprey rbcs was also evaluated using mass spectrometry. The bicarbonate permeability of the lamprey rbc membrane was an order of magnitude lower than that of trout rbcs. Taken together, these results indicate that the gene for the AE protein is indeed present in lampreys, but it is not expressed in the rbc. Moreover, the process of CO2 transport in lamprey probably does not involve bicarbonate transport across the rbc membrane.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-136X
    Keywords: Anion movements ; Chloride/bicarbonate exchange ; Red cell proteins ; AE1 or band 3 ; Petromyzon marinus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Physiological and immuno-blotting experiments were used to determine whether the red blood cell membrane of a primitive vertebrate, the sea lamprey Petromyzon marinus, contained a counterpart similar to the vertebrate anion exchange protein known as AE1 or band 3. Results of the physiological experiments which measured CO2 production after adding H14CO 3 - to the extracellular saline, indicated significant transmembrane bicarbonate movement in lamprey blood which unlike that in most vertebrates, was insensitive to inhibition by 4,4′ diisothiocyanatostilbene-2,2′ disulfonic acid. The present study also showed that lamprey red blood cells possess acetazolamide-sensitive carbonic anhydrase which is an important component of CO2 production by vertebrate red blood cells. Polyclonal immunoglobulins against a 12 amino acid domain in the C-terminus of the mouse AE1 recognized a trout red blood cell membrane protein with a relative molecular mass of 97 kDa, but failed to immunoreact with any membrane proteins from the red blood cells of lamprey. Antibodies against trout AE1 immunoreacted with trout red blood cell membrane proteins of approximately 97 kDa, 200 kDa and 〉200 kDa. Interestingly, only a 200-kDa membrane protein from the red blood cells of the primitive lamprey immunoreacted with the trout anti-AE1 immunoglobulin proteins. Therefore, lamprey red blood cells appear to possess an AE1-like protein that may be physiologically different than that in most other vertebrates.
    Type of Medium: Electronic Resource
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