A consensus amino-acid sequence repeat in Torpedo and mammalian Ca2+-dependent membrane-binding proteins

A group of calcium-binding proteins which bind to biomembranes has recently been identified in widely different cells and tissues (refs 1-7, reviewed in ref. 8). Three of these proteins (p70, p36 and p32.5) cross-react with antiserum to calelectrin, a Ca2+-binding protein (relative molecular mass 34,000 (34K] from the ray Torpedo marmorata, giving rise to their designation as calelectrin-related proteins. We now report that calelectrin, p36 and p32.5 contain a 17-amino-acid consensus sequence which is conserved and present in multiple copies. We suggest that this sequence may be common to other members of this new group of Ca2+-binding proteins and may underlie their unusual mode of combination with biomembranes.     

Alkaloid studies XXVI. The constitution of pyrifolidine

Zusammenfassung Die Struktur desAspidosperma-Alkaloids Pyrifolidin (I) wird durch Protonresonanz und durch Vergleich mit Aspidospermin und Aspidocarpin bewiesen. Dieses Alkaloid ist in seiner absoluten Konfiguration ein Antipode des Aspidospermins.

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Paper XXV,C. Djerassi, A. A. P. G. Archer, T. George, B. Gilbert, J. N. Shoolery, andL. F. Johnson, Exper.16, 532 (1960).

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Acknowledgement. Financial support has been provided by grant H-5048 of the National Heart Institute, National Institutes of Health (U.S. Public Health Service), and by the Conselho Nacional de Pesquisas (Brazil). The postdoctorate research fellowship ofB. Gilbert in Rio de Janeiro was financed from a grant of the Rockefeller Foundation in support of a collaborative research program between Stanford University and the Instituto de Quimica Agricola, Rio de Janeiro (Brazil).     

Relationship between science and technology

Do economic advances spring directly from fundamental scientific discoveries? The early history of the transistor suggests that the situation is not nearly so simple as this.     

Immobilization of chicken liver fructose 1,6-bisphosphatase on CNBr-activated Sepharose

Chicken liver fructose 1,6-bisphosphatase is readily immobilized on CNBr-activated Sepharose. The immobilization alters some enzymatic properties. They include broader pH activity curve, loss of activation by K+ or NH+4, increased resistance to inactivation by trypsin, decreased sensitivity to AMP inhibition, and loss of cooperative interaction among AMP-binding sites. The immobilized enzyme retains about 38% or 19% of the specific activity of the native enzyme when the activity is measured in the absence or presence of K+, respectively.