Haemolysis of rabbit erythrocytes by a lectin from the seeds of<Emphasis Type="Italic">Croton tiglium</Emphasis>

The kinetics of haemolysis of rabbit erythrocytes byCroton tiglium lectin was studied as a function of concentration of the lectin and erythrocytes. The length of the prelytic period decreased with increasing lectin concentrations, indicating that the secondary events at the membrane which follow the binding of the lectin to cell surface carbohydrate receptors are accelerated at higher surface concentrations of the lectin. The rate or extent of haemolysis was not affected by the inclusion of ions like K⁺, Ca²⁺ and Mg²⁺ in the medium or by the substitution of ionic medium by a non-ionic medium. The inhibition of haemagglutination and haemolysis of rabbit red cells byCroton tiglium lectin by antilectin rabbit serum was observed. A possible mechanism of haemolysis by the lectin is discussed.     

Plant lectins specific for N-acetyl-β-D-galactosamine

N-Acetyl-D-galactosamine in β-linkage being ubiquitous in cell surface glycoproteins, their interaction with lectins specific for this sugar moiety may be a significant event in cell adhesion phenomena. This article discusses the common β-N-acetyl galactosamine-specific lectins, with particular stress on the lectin from winged beans (Psophocarpus tetragonolobus).     

Role of Peroxidase when Hydroxyproline-rich Protein in Plant Cell Walls is increased by Ethylene

Ethylene may control the growth of plant cells by regulating hydroxylation of specific wall proteins.     

Genetic Control of Variable and Constant Regions of Immunoglobulin Heavy Chains

IMMUNOGLOBULIN polypeptide chains consist of two well defined regions designated the “variable region” and the “constant region”. Whereas great diversity exists in amino-acid sequences of variable regions, the constant regions of a given subclass of heavy chains (C_H)^* are essentially invariant in sequence^{1, 2}. Exceptions are the allelic forms, such as the rabbit allotypes A14 and A15^{3, 4}, where a threonine-alanine interchange occurs in the constant region of γ chains (Appella, Chersi, R. G. M. and Dubiski, in preparation). The markers unique to a chains (for example, A14-A15) are closely linked to allotypic markers at the a locus (a1, a2, a3)^{3, 4} which seem to be present on four different Ig heavy chain classes (α, γ, ε, µ)^5–7. These puzzling observations can be explained if the a locus determinants are variable region markers which reflect genetically controlled differences in some relatively constant residues within the V_H region sequences⁷.     

Demonstration of an “Excitation-Contraction Recoupling” Mechanism in Mammalian Ventricular Myocardium

A PROCESS called “excitation-contraction coupling” has been generally accepted to take place only in the direction of excitation to contraction. Through this mechanism a propagated action potential initiates an active state in skeletal or cardiac muscle and the muscle contracts. We propose that, in the mammalian ventricular myocardium at least, the process is not unidirectional and an important reverse coupling between the contractile system and the excitable plasma membrane has been overlooked. Through this feedback interaction the mode of contraction (that is, isotonic or isometric) not only determines the instantaneous electrical state of the plasma membrane, but also influences the mechanical events of the subsequent beats. Thus when Kaufmann et al.¹ recorded intracellular action potentials from cat papillary muscle, the time course of the repolarization was altered depending on the mode of contraction. Some kind of contraction-excitation feedback has also been suggested by Stauch² and Lab^3,4. They showed a difference in the shape of the monophasic action potential, as recorded by a suction electrode, when comparing isotonic and isovolumic contraction of the intact ventricle. But their experimental conditions did not allow satisfactory analysis of the phenomenon.     

The Structure of Calf Liver Cytochrome <Emphasis Type="Italic">b</Emphasis><Subscript>5</Subscript> at 2.8 Å Resolution

CYTOCHROME b₅ is a haem-containing protein in the microsomes of liver tissue. It interacts specifically with a flavo-protein, cytochrome b₅ reductase, which catalyses the transfer of electrons from NADH to the haem iron of the cytochrome¹. The microsomal cytochrome b₅ system has been implicated in fatty acid desaturation reactions² and a similar system in erythrocytes may catalyse the reduction of methaemoglobin³. Calf liver cytochrome b₅, solubilized by pancreatic lipase, has a molecular weight of 11,000 and consists of ninety-three amino-acids in the sequence shown in Fig. 1 (refs. 4 and 5). The haem group is non-covalently bound to the protein and can be removed reversibly by acid acetone treatment⁶.     

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.     

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.