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A cladistic phylogeny of the genus Littorina (Gastropoda): implications for evolution of reproductive strategies and for classification (1990)

Reid, David G.

Springer

Hydrobiologia 193 (1990), S. 1-19

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ISSN: 1573-5117

Keywords: biogeography ; Atlantic ; Pacific ; reproductive strategy ; larval development

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Gross anatomical characters of all 18 species of Littorina are used to construct a phylogenetic hypothesis for the genus, by the method of cladistic analysis. The resulting cladogram suggests that of the four subgenera of Littorina, one (Littorina) is paraphyletic. It is uncertain whether the genus Mainwaringia should be included in Littorina. It is shown that the non-planktotrophic Littorina species in the northern Atlantic comprise a monophyletic group, with the sister-species L. kurila and/or L. subrotundata in the northern Pacific. Invasion of the Atlantic by a minimum of two Pacific species, across the Arctic migration route established during the late Cenozoic, is sufficient to account for the modern distribution of the subgenera Littorina and Neritrema. The importance of the cladogram as a basis for hypotheses of adaptation is illustrated by a discussion of spawn and development in Littorina.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00028062

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Calmodulin discriminates between the two enantiomers of the receptor-operated calcium channel blocker sk&f 96365: A study using 1H-NMR and chiral HPLC (1990)

Reid, David G. ; MacLachlan, Lesley K. ; Robinson, Simon P. ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Chirality 2 (1990), S. 229-232

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ISSN: 0899-0042

Keywords: receptor-operated calcium channel antagonist ; 1H NMR ; chiral HPLC ; calmodulin ; Chemistry ; Organic Chemistry

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: 1H nuclear magnetic resonance at 360 MHz shows that SK&F 96365 (1-{β-[3-(p-methoxyphenyl)-propyloxy]-p-methoxyphenethyl}-1H- imidazole hydrochloride), an antagonist of mammalian receptor-operated calcium channels, interacts with the calcium-binding regulatory protein calmodulin (CaM). This may be inferred by a number of chemical shift changes in the spectrum of the calcium-saturated protein induced by addition of the compound. Moreover, two well-resolved singlets corresponding to the 2-proton of the SK&F 96365 imidazolium moiety are observed in the spectrum over a wide range of protein:compound ratios. Separation of rac SK&F 96365 into its two enantiomers by high-performance liquid chromatography on a cellulose tris (4-methylbenzoate) column enabled us to show that the doubling of this NMR signal in the presence of CaM is due to a propensity of the protein to distinguish between the two optical isomers of the compound.

Additional Material: 3 Ill.