Structure of the “Peroxy-Y Base” from Liver tRNA<Superscript>Phe</Superscript>

WE wish to report that reconstituted sperm whale myoglobin prepared by the method of Breslow¹ (except that pH 2 was found sufficient to remove all the haem) (I) crystallizes² in a different habit from those prepared by the method of Rossi-Fanelli et al.³ (II) using haemin of Sigma lot 77B-0220 and our own ⁵⁷Fe photoporphyrin preparation and the native myoglobin (III). Although all three form type A³ monoclinic prisms, the best developed plane is [001] for II and III, it is [100] for I. There seems to be great interest in reconstituted haemoproteins^4,5, so it is important that crystallization habit may be a sensitive test for subtle changes in protein structures.     

Glucagon Affinity Absorbents: Selective Binding of Receptors of Liver Cell Membranes

AFFINITY chromatography has been used in the rapid isolation of enzymes, antibodies, antigens and other ligand-binding proteins^1–6. Selective adsorbents with biological specificity perhaps may best be used in the resolution and isolation of complex biological structures and important regulatory macromolecules present in cells in very low amounts. For example, polypeptide and steroid hormone receptors, drug receptors, transport proteins and repressor molecules may be well suited for study by this technique because they display specific binding functions with a high degree of affinity.     

Role of the Galactose Binding Protein in Chemotaxis of <Emphasis Type="Italic">Escherichia coli</Emphasis> toward Galactose

The galactose binding protein is the part of the galactose chemoreceptor which recognizes the attractants galactose, glucose and a number of structurally related chemicals.     

Additional Nucleotide Sequences in Precursor 16S Ribosomal RNA from <Emphasis Type="Italic">Escherichia coli</Emphasis>

MATURE 5S, 16S and 23S ribosomal RNA species present in E. coli ribosomes are the end products of complex biosyn-thetic pathways. They are formed by reduction in length, and methylation of longer RNA chains transcribed on the ribosomal RNA cistrons of E. coli DNA. While these modifications take place the ribosome structure is formed by progressive addition of ribosomal proteins and conformational changes in the resulting ribonucleoprotein precursor particles¹.     

Ribosomes,G-factor and Siomycin

G-factor interacts with the 50S ribo-somal subunit at a site which is distinct from the peptidyl transferase centre and which is inactivated by siomycin.     

Passive Haemagglutination Test for Anti-rhinovirus Antibodies

The use of chromic chloride as a coupling reagent has made it possible to coat red cells with rhinovirus protein. This is shown by immunofluorescence, electron microscopy and immunocolloidal experiments.     

Failure of Neuraminidase to unmask Histocompatibility Antigens on Trophoblast

DURING outbred pregnancy the mother is exposed to genetically foreign tissue because the offspring inherits transplantation antigens from the father. The survival of the foetus is ensured by the intervention of the trophoblast which does not express transplantation antigens between mother and foetus: mouse trophoblast is not rejected even when transplanted into immune recipients^1,3. The mechanism of this failure to express histocompatibility antigens is not understood^1–4, but Kirby et al. have suggested that the extracellular fibrinoid surrounding trophoblast cells is involved^5,6. Currie has suggested that the thick sialomucinous glycocalyx of the trophoblast cell might “mask” the histocompatibility antigens on the trophoblast^7,8 and has demonstrated that neuraminidase unmasked these antigens⁸. Our experiments, however, show that trophoblast incubated with neuraminidase cannot sensitize allogeneic mice to donor histocompatibility antigens. Furthermore, pretreatment of trophoblastic implants with neuraminidase did not interfere with their proliferation and growth in highly immune allogeneic recipients.     

Constant Production of Type C Virus Particles in a Continuous Tissue Culture derived from Pleural Effusion Cells of a Lymphoma Patient

PARTICLES resembling viruses were first observed in organs of mice with spontaneous leukaemia and in thin sections of a biopsy specimen from a lymph node of a patient with acute lymphocytic leukaemia by Dmochowski and Grey¹. They also found them in some biopsy specimens of lymph nodes and bone marrows before and after growth in tissue culture^2,3,8. Recent reports have described the presence of type C virus particles in other human tumours including liposarcoma⁴, osteosarcoma^5,6, giant cell tumour⁹, rhabdomyosarcoma (unpublished results of L. D. and E. S. P.) and breast carcinoma⁷.     

Antigenic Heterogeneity of Human IgD Immunoglobulins

SUBCLASSES of the three major classes of human immunoglobulins, IgG, IgA and IgM, are recognized: four of IgG are well defined^1,2 and at least two of IgA^3–5 and two of IgM^6,7 have been demonstrated. This communication presents evidence for the existence of an antigenic heterogeneity in the heavy chains of IgD, which may also be indicative of subclasses within this class of immunoglobulin.     

Coexistence of Intraspecies and Interspecies Specific Antigenic Determinants on the Major Structural Polypeptide of Mammalian C-type Viruses

THE report of a shared viral antigen (termed gs-3) among mammalian C-type viruses from four species¹, extending an earlier report of cross reactivity between mouse and cat viral antigens², has far reaching implications in the search for human cancer viruses or their gene products. The report is confirmed both by the data presented here and also by the data obtained by another laboratory³. Our gel diffusion assays using various selected sera against mouse, hamster and cat crude and purified C-type viral antigens indicate that the cross reactive antigenic determinants are specifically present on the major structural polypeptide of C-type viruses. The polypeptide also carries species specific determinants. These conclusions are drawn from complement fixation and gel diffusion tests using six types of antisera (either individual sera or pools) prepared as described in Table 1.