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  • Freezing  (1)
  • cDNA
  • 3H
  • AC-ECD
  • Springer  (2)
  • Munksgaard International Publishers
  • 1990-1994  (2)
Collection
Publisher
  • Springer  (2)
  • Munksgaard International Publishers
Years
Year
  • 1
    ISSN: 1432-136X
    Keywords: Amphipoda ; Crustacea ; Haemocyanin ; Freezing ; Inorganic effectors ; Urate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The effect of variations in [K], [Ca], [Mg], [NaCl], and [urate] on the in vitro O2 binding properties of haemocyanin (Hc) from three talitroidean species, viz. the aquatic Apohyale pugettensis, the semi-terrestrial Megalorchestia californiana, and the semi-/euterrestrial Traskorchestia traskiana were studied. Freezing altered the cooperativity of Hc from A. pugettensis and M. californiana but not T. traskiana. Variations in [NaCl], [K], and [Mg] had no effect on cither O2 affinity or cooperativity of the Hc except for A. pugettensis Hc where an increase in [Mg] resulted in an increase in both O2 affinity and cooperativity. Increasing [Ca] or [urate] increased O2 affinity of both A. pugettensis and M. californiana but not T. traskiana Hc. These effects were most marked in A. pugettensis. The results suggest a negative correlation between sensitivity to Hc effectors and the degree of terrestrial adaptation of a particular amphipod species.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4919
    Keywords: cDNA ; human ; placenta ; immunoglobulin ; pregnancy-specific β1-glycoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Three cDNAs encoding members of the pregnancy-specific β1-glycoprotein (PSG) family were isolated from human term placental cDNA library. All three cDNAs encode proteins with similar domain structure. There is a leader sequence of 34 amino acids followed by an N-domain of 109 amino acids. Immediately after the N-domain are one or two copies of a repeating A-domain of 93 amino acids, a B-domain of 85 amino acids and a C-domain of variable size. The proteins are highly hydrophilic. However, one of them has an 81-amino acid C-domain which is very hydrophobic and could potentially serve as a membrane attachment site. The putative cell-cell recognition tripeptide, Arg-Gly-Asp, is present in the N-domain of two of the proteins. Partial sequence of one of the cDNAs has been found in HeLa cells while cDNAs highly homologous to two of the cDNAs have been found in the fetal liver. Functional roles of the PSG proteins basing on their structure are proposed.
    Type of Medium: Electronic Resource
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