Prevention of enteral radiocesium absorption by hexacyanoferrates(II) in piglets

The efficacy of different hexacyanoferrates(II) in preventing the enteral absorption of 134Cs was studied in piglets. As compared to the controls, oral application of 134Cs together with KFe[Fe(CN)6], NH4Fe[Fe(CN)6], or Fe4[Fe(CN)6]3 resulted in a strong reduction of the 134 Cs-uptake by more than 97%. The decrease in enteral absorption depends on the dose of administered hexacyanoferrate(II), whereas differences between the compounds under study were small. The biological half-life of 134Cs in non-hexacyanoferrate(II) treated piglets was 21.6 +/- 3.3 days (mean +/- SD).     

High molecular transport proteins for JH-III in insect hemolymph

Summary Using two independent techniques, ultracentrifugation in a KBr-gradient, and native pore polyacrylamide gel electrophoresis in combination with [³H]-epoxyfarnesyldiazoacetate photoaffinity labeling, we showed that in the hemolymph ofPeriplaneta americana, and probably also inLeptinotarsa decemlineata JH-III binds to the lipophorin, whereas inLocusta migratoria JH-III binds to a different protein.     

Complementary DNA for a novel human interleukin (BSF-2) that induces B lymphocytes to produce immunoglobulin

When stimulated with antigen, B cells are influenced by T cells to proliferate and differentiate into antibody-forming cells. Since it was reported that soluble factors could replace certain functions of helper T cells in the antibody response, several different kinds of lymphokines and monokines have been reported in B-cell growth and differentiation. Among these, human B-cell differentiation factor (BCDF or BSF-2) has been shown to induce the final maturation of B cells into immunoglobulin-secreting cells. BSF-2 was purified to homogeneity and its partial NH2-terminal amino-acid sequence was determined. These studies indicated that BSF-2 is functionally and structurally unlike other known proteins. Here, we report the molecular cloning, structural analysis and functional expression of the cDNA encoding human BSF-2. The primary sequence of BSF-2 deduced from the cDNA reveals that BSF-2 is a novel interleukin consisting of 184 amino acids.     

Secretion of cytokinins in vivo and in vitro byAlternaria brassicicola and their role in pathogenesis

Summary Formation of green islands in the host (mustard leaves) beneath the infection-drops containing germinating conidia ofAlternaria brassicicola (Schw.) Wiltsch. has been correlated with the secretion of cytokinins by the pathogen.A. brassicicola also synthesized cytokinins in the liquid synthetic medium. Cytokinins produced in vitro were extracted, and their application on the detached mustard leaves evoked the formation of green islands.     

Analysis of T-cell subsets in rejection of Kb mutant skin allografts differing at class I MHC

The T-cell subpopulations which initiate and mediate tissue allograft rejection remain controversial. In the present study we attempted to identify the phenotype and function of the T-cell subset(s) primarily responsible for the rejection of skin allografts differing at a single class I locus in the major histocompatibility complex (MHC). We found that the rejection rates by B6 mice (H-2b) of four different class I mutant (Kbm) skin allografts form a distinct hierarchy. This hierarchy correlates strikingly and uniquely with the relative precursor frequencies of Lyt2+ interleukin-2-secreting T-helper cells reactive against the various Kbm mutants. To investigate the role of Lyt2+ T cells in the rejection of class I-disparate skin allografts directly, H-2b nude mice were engrafted with Kbm skin allografts and then reconstituted with L3T4+ or Lyt2+ T-cell subpopulations from syngeneic H-2b mice. Lyt2+ T cells were observed to be both necessary and sufficient for the rejection of class I-disparate Kbm skin allografts, whereas L3T4+ T cells were neither necessary nor sufficient. These results identify the Lyt2+ interleukin-2-secreting T-cell subset as the critical cell type determining the rejection rate of class I-disparate Kbm skin allografts.     

The essential light chains constitute part of the active site of smooth muscle myosin

Myosin, a major contractile protein, characteristically possesses a long coiled-coil alpha-helical tail and two heads. Each head contains both an actin binding site and an ATPase site and is formed from the NH2-terminal half of one of the two heavy chains (relative molecular mass, Mr, 200,000) and a pair of light chains; the so-called regulatory and essential light chains of approximately Mr 20,000 each. Recently we have identified Trp 130 of the myosin heavy chain from rabbit skeletal muscle as an active-site amino-acid residue after labelling with a new photoaffinity analogue of ADP, N-(4-azido-2-nitrophenyl)-2-aminoethyl diphosphate (NANDP). Nonspecific labelling was eliminated by first trapping NANDP at the active site with thiol crosslinking agents. Exclusive labelling of the heavy chains with no labelling of the light chains agreed with previous findings that the heavy chains alone contain the actin-activated Mg-ATPase activity of rabbit skeletal myosin. Here we report similar photolabelling experiments with smooth muscle myosin (chicken gizzard) in which 3H-NANDP is trapped at the active site with vanadate and which show that both the heavy chains and the essential light chains are labelled. The results indicate that both chains contribute to the ATP binding site and represent the first direct evidence for participation of the essential light chains in the active site of any type of myosin.     

Recognition of myelin-associated glycoprotein by the monoclonal antibody HNK-1

Myelin-associated glycoprotein (MAG) is a quantitatively minor component in both peripheral and central myelin sheaths that is thought to have a role in cell-cell interactions within the nervous system. We show here that a mouse monoclonal antibody, HNK-1, which is directed against human natural killer cells also recognizes an antigenic determinant of human central and peripheral nervous system white matter by immunoperoxidase staining of tissue sections. Immunoblot analysis of myelin proteins and purified extracted MAG indicates that the antigen recognized is MAG.     

Absence of cooperative haemoglobin-oxygen binding in Sphenodon, a reptilian relict from the Triassic

It is generally accepted that the sigmoidal nature of the haemoglobin-oxygen dissociation curve (ODC) is necessary for efficient oxygen transport in terrestrial vertebrates because it allows large volumes of oxygen to be bound or released for relatively small changes in the partial pressure of oxygen (PO2) in the blood. Furthermore, the amount of oxygen to tissues is increased by hydrogen ions produced from the dissociation of carbon dioxide in solution. The generality of these key features of cooperative oxygen binding and the Bohr effect holds for reptiles, birds and mammals, including representatives with special respiratory requirements for diving, burrowing and living at high altitude. Sphenodon punctatus is the sole surviving representative of the ancient order of 'beakhead' reptiles (order Rhynchocephalia) which were once widely distributed during the Triassic period before the spectacular radiation of dinosaur faunas. We have now investigated the oxygen transporting properties of blood from Sphenodon and find that the ODC is hyperbolic, with a high affinity for oxygen and very small Bohr effect. This combination of characteristics is unique among terrestrial vertebrates and accords with a low demand for oxygen and limited scope for aerobic activity.     

The Tetrahymena ribozyme acts like an RNA restriction endonuclease

A shortened form of the Tetrahymena self-splicing ribosomal RNA intervening sequence acts as an endoribonuclease, catalysing the cleavage of large RNA molecules by a mechanism involving guanosine transfer. The sequence specificity approaches that of the DNA restriction endonucleases. Site-specific mutagenesis of the enzyme active site alters the substrate sequence specificity in a predictable manner, so that endoribonucleases can be synthesized to cut at a variety of tetranucleotide sequences.