Receptors for thymosin fraction V on rat thymic lymphocytes

Summary Binding by rat thymus lymphocytes of thymosin V, labeled with colloidal gold, was studied. Under the experimental conditions employed at least 2.8% cells exhibited thymosin binding sites.This article originally appeared in Experientia 38 (5) 1982, p. 618 but was accompanied by imporperfigures. Supported by Polish Academy of SciencesThe authors thank Dr A.L. Goldstein for the gift of thymosin. Also are grateful to Dr J. Jaroszewski for helpful discussion.     

Binding of iron by rat placental tissues

Zusammenfassung Nachweis, dass das Eisenbindungsvermögen der Dottersackplacenta bedeutend grösser ist als bei der chorioallantoiden Placenta und dass diese auch unter der Einwirkung von den Stoffwechsel beeinflussenden Stoffen ein verschiedenes Verhalten zeigt.

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This work was supported by U.S. Public Health Service Grant No. HD05016 and Predoctoral Fellowship Grant No. FO1-DE41063 to R.J.B.G.     

A simple method for the preparation of antibodies to the mitochondrial biotin-dependent carboxylases

Heterologous antiserum to the 3 biotin-dependent carboxylases was prepared by selective removal of these enzymes from human liver on an avidin-sepharose column. A carboxylase-avidin-sepharose matrix was used as an antigen to produce anti-carboxylase antibodies. The resultant antisera can be used to purify the specific carboxylases, to prepare monoclonal antibodies to these enzymes or to study inherited carboxylase deficiencies and biotin-dependent intermediary metabolism.     

Crystal structure of a hairpin ribozyme-inhibitor complex with implications for catalysis

The hairpin ribozyme catalyses sequence-specific cleavage of RNA. The active site of this natural RNA results from the docking of two irregular helices: stems A and B. One strand of stem A harbours the scissile bond. The 2.4 A resolution structure of a hairpin ribozyme-inhibitor complex reveals that the ribozyme aligns the 2'-OH nucleophile and the 5'-oxo leaving group by twisting apart the nucleotides that flank the scissile phosphate. The base of the nucleotide preceding the cleavage site is stacked within stem A; the next nucleotide, a conserved guanine, is extruded from stem A and accommodated by a highly complementary pocket in the minor groove of stem B. Metal ions are absent from the active site. The bases of four conserved purines are positioned potentially to serve as acid-base catalysts. This is the first structure determination of a fully assembled ribozyme active site that catalyses a phosphodiester cleavage without recourse to metal ions.