Ultrastructure of human myeloma cells studied by peroxidase conjugated antibodies directed to human immunoglobulin component chains

Zusammenfassung Menschliche Myelomazellen wurden immunchemischelektronenoptisch untersucht. Durch die Behandlung mit peroxidasekonjugiertem Antikörper gegen die Immunoglobuline H- oder L-Kette wurde keine H-Kette beobachtet.     

Immunoglobulin light chains, glycosaminoglycans, and amyloid

Immunoglobulin light chains are the precursor proteins for fibrils that are formed during primary amyloidosis and in amyloidosis associated with multiple myeloma. As found for the approximately 20 currently described forms of focal, localized, or systemic amyloidoses, light chain-related fibrils extracted from physiological deposits are invariably associated with glycosaminoglycans, predominantly heparan sulfate. Other amyloid-related proteins are either structurally normal, such as beta2-microglobulin and islet amyloid polypeptide, fragments of normal proteins such as serum amyloid A protein or the precursor protein of the beta peptide involved in Alzheimer's disease, or are inherited forms of single amino acid variants of a normal protein such as found in the familial forms of amyloid associated with transthyretin. In contrast, the primary structures of light chains involved in fibril formation exhibit extensive mutational diversity rendering some proteins highly amyloidogenic and others non-pathological. The interactions between light chains and glycosaminoglycans are also affected by amino acid variation and may influence the clinical course of disease by enhancing fibril stability and contributing to resistance to protease degradation. Relatively little is currently known about the mechanisms by which glycosaminoglycans interact with light chains and light-chain fibrils. It is probable that future studies of this uniquely diverse family of proteins will continue to shed light on the processes of amyloidosis, and contribute as well to a greater understanding of the normal physiological roles of glycosaminoglycans.     

Intramuscular comparison of myosin isozymes and light chains in rat extensor digitorum longus muscle

Summary Complete muscle cross sections were obtained from the proximal and distal third regions of ten rat extensor digitorum longus muscles. Electrophoretic methods were then used to quantify the various myosin isozymes and light chains in each muscle specimen. The results demonstrated that the relative distribution of the various myosin isozyme and light chain variables do not vary significantly between the two sampling regions.     

Intramuscular comparison of myosin isozymes and light chains in rat extensor digitorum longus muscle

Complete muscle cross sections were obtained from the proximal and distal third regions of ten rat extensor digitorum longus muscles. Electrophoretic methods were then used to quantify the various myosin isozymes and light chains in each muscle specimen. The results demonstrated that the relative distribution of the various myosin isozyme and light chain variables do not vary significantly between the two sampling regions.     

A study of invertebrate actins by isoelectric focusing and immunodiffusion

Actin isolated from various invertebrate phyla comigrates with the beta-form of vertebrate smooth muscle actin. However, invertebrate actins are not identical, since antibodies to insect-actin will not crossreact with the other species.     

A study of invertebrate actins by isoelectric focusing and immunodiffusion

Summary Actin isolated from various invertebrate phyla comigrates with the -form of vertebrate smooth muscle actin. However, invertebrate actins are not identical, since antibodies to insect-actin will not crossreact with the other species.This work was supported by the Deutsche Forschungsgemeinschaft (Ste 105/19+20).We wish to thank Dr. R. Whalen, Inst. Pasteur, Paris, for introducing us to the technique of I.E.F.     

Effect of phosphorylation of myosin light chains on interaction of heavy meromyosin with regulated F-actin in ghost fibers

Summary The binding of phosphorylated heavy meromyosin to regulated F-actin in ghost fibers at high Ca²⁺ concentration increases, and at low Ca²⁺ concentration decreases, the anisotropy of intrinsic tryptophan fluorescence of F-actin. The effect is opposite to the effect of the binding of dephosphorylated heavy meromyosin.     

Isoelectric focusing of neuraminidase

Zusammenfassung Die isoelektrischen Punkte der Neuraminidasen vonVibrio cholerae (pH 4.80) undClostridium perfringens (pH 4.95) wurden mittels isoelektrischer Fokusierung bestimmt. Neuraminidasen zwei verschiedener Influenzaviren (A₂/Aichi/68 und B/Mass/66) wurden entsprechend analysiert. Die Virus-Neuraminidasen waren Heterogen und hatten wesentlich höhere isoelektrische Punkte als die bakteriellen Enzyme.     

Effect of phosphorylation of myosin light chains on interaction of heavy meromyosin with regulated F-actin in ghost fibers

The binding of phosphorylated heavy meromyosin to regulated F-actin in ghost fibers at high Ca2+ concentration increases, and at low Ca2+ concentration decreases, the anisotropy of intrinsic tryptophan fluorescence of F-actin. The effect is opposite to the effect of the binding of dephosphorylated heavy meromyosin.     

Electrophoretic heterogeneity exhibited by the S-allele specific glycoproteins ofBrassica

Summary A number of self-incompatibility genotypes ofB. oleracea were analyzed by sensitive electrophoretic procedures. Members of the class of S-allele specific glycoproteins that increase in correlation with the onset of the incompatibility response were resolved into several components on SDS gels. The implications of this molecular heterogeneity are discussed in relation to S locus function.This work was supported by NSF grant No. PCM 8118035. The authors acknowledge the assistance of Dr Marilou McLaughlin, Coordinator of Sponsored Research, SUNY, Cortland, and thank Carl Burr, Delia Baroni, and Raymond Nagell for assistance in photography.     

Ultrastructure of the salivary gland chromosome as revealed by electron microscopy

Zusammenfassung An ultradünnen Schnittpr?paraten von Speicheldrüsenchromosomen (Drosophila melanogaster) und an entsprechenden Quetschpr?paraten (Drosophila virilis) wurde elektronenmikroskopisch festgestellt: Die Chromomeren und Chromonemata bestehen aus Filamenten mit Schraubenwindungen vom ?paran?mischen? Typus. Es ist wahrscheinlich, dass die Windungen der beiden Filamente in der entgegengesetzten Richtung ranken.

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The substance of this article was present in 1956 at the International Genetics Symposia in Tokyo.     

Functions of nuclear bodies as revealed by ultrastructural autoradiography and cytochemistry

Summary The simple nuclear body containing a few RNA particles appears through the nuclear pores in the cytoplasm, originating from the nucleolus. The complex nuclear body consisting mainly of RNA components is highly active in the incorporation of RNA precursors. Accordingly, the appearance of nuclear bodies may be related either to transport to the cytoplasm of nucleolar components or to the enhancement of rRNA synthesis.