All Superparticles are BPS

The generic action for an N-extended superparticle in D-dimensional Minkowski spacetime is shown to have "hidden" supersymmetries (related by "dualities" to the manifest supersymmetries) such that the full supersymmetry algebra is BPS-saturated; the exceptions (which include, trivially, the massless case) are those for which the manifest supersymmetry algebra is already BPS-saturated. Moreover, it is shown that any "non-BPS" superparticle action is a gauge-fixed version of the "BPS" superparticle action for which all supersymmetries are manifest. An example is the N=1 massive D=10 superparticle, which actually has N=2 supersymmetry and is equivalent to the action for a D0-brane of IIA superstring theory.Comment: 13 pages. Minor improvements plus new reference in v

Equivalence of 3D Spinning String and Superstring

We perform a light-cone gauge quantization of the Ramond closed spinning string in three spacetime dimensions (3D). The spectrum is Lorentz invariant and identical to that of the 3D Green-Schwarz closed superstring with ${\cal N}=2$ space-time supersymmetry, quantized in light-cone gauge.Comment: 15 pages. Revised to include discussion of modular invarianc

Electrophoretic Analysis of the Serum Proteins of Normal Newborn Infants

The protein components of the serum of newborn infants have occupied the attention of few investigators. McKhann and Kapnick (1) pointed out that newborn infants show an immunity to many diseases during the first months of life. Electrophoretic studies carried out by Tiselius and Kabat (2) demonstrated that the gamma globulin fraction of the serum contains the antibodies. Other investigators (3, 4, 5) reported a low ratio of albumin to globulin in the serum of newborn infants. The increase in globulin was shown to be mainly in the gamma globulin component (6, 7, 8, 9). Since the technique of filter paper electrophoresis is adaptable to small quantities of serum, it is a useful method for the fractionation of the proteins of the serum of newborn infants. This study was undertaken to determine normal values for the serum protein components of newborn infants employing the technique of paper and free electrophoresis. It is hoped that these normal values will find use as a base line in further studies of serum proteins in newborn infants

The Interaction Between the Urinary Trypsin Inhibitor and Trypsin

Gel filtration and disc electrophoresis were used as simple and fast techniques for the investigation of the interaction and stoichiometry between UTI and trypsin. UTI appears to possess only a single trypsin binding site. The nature of the interaction between the inhibitor and enzyme appears to be dependent on the concentration ratio of the reactants. When UTI is in excess molar concentration, a single binary complex with trypsin of mol. wt. 95,000 is observed. In the presence of a molar excess of enzyme, this macromolecule is no longer observed, but proteins of mol. wt. 41,000 and 20,000 result. The possibility that UTI may be hydrolyzed to a partially degraded active fragment by the excess enzyme resulting in the formation of a modified inhibitor enzyme complex is proposed

Electrophoretic Analysis of the Proteins of Body Fluids in Various Disease States

Plasma, serum, and body fluid specimens (pleural fluid, ascitic fluid, synovial fluid, edema fluid, hydrocele fluid, cyst fluid, lymph, bile, and subdural fluid) from patients with heart disease, carcinoma, liver disease, and arthritis, were subjected to electrophoretic analysis. A decrease in plasma albumin and an increase in globulin components occurred in the disease conditions. In most instances the albumin and gamma globulin were higher, the α1 globulin the same, and the α2 and β globulin and fibrinogen in lower concentration in the fluid than in the corresponding plasma specimen. The distribution of the protein components between the plasma and fluid is explained on the basis of their molecular weights

Electrophoretic Studies of the Proteins of Plasma and Ascitic Fluid in Cirrhosis

A series of plasma and ascitic fluid specimens withdrawn from patients with cirrhosis, and a series from one patient over a seven-week period prior to his death, were subjected to electrophoretic analysis. The results indicate a qualitative similarity between plasma and ascitic fluid protein patterns. In most instances, the ascitic fluid contained more albumin, alpha1 and gamma globulins than the plasma, whereas the plasma was richer in alpha2 and beta globulins and fibrinogen. Based on the molecular weights of the protein fractions, the values indicate that selective protein enrichment of ascitic fluid may be related to the molecular size of the protein components

A Comparison of Plasma Protein Fractions by Kjeldahl and Biuret Analysis and Refractive Index Measurements

In electrophoretic studies of serum and plasma the concentration of protein in the various fractions is often expressed in absolute values. These are commonly obtained by calculation from the percentage distribution of the components and the total protein content of the serum or plasma. Although this practice is widespread there is no assurance that the values obtained reflect a true measure of the protein content of the individual components. It is readily apparent from the divergent results obtained by the technique of paper electrophoresis that the major components of serum contain varying concentrations of protein, lipids and carbohydrates and exhibit a varying response to protein dyes

Routh's procedure for non-Abelian symmetry groups

We extend Routh's reduction procedure to an arbitrary Lagrangian system (that is, one whose Lagrangian is not necessarily the difference of kinetic and potential energies) with a symmetry group which is not necessarily Abelian. To do so we analyse the restriction of the Euler-Lagrange field to a level set of momentum in velocity phase space. We present a new method of analysis based on the use of quasi-velocities. We discuss the reconstruction of solutions of the full Euler-Lagrange equations from those of the reduced equations.Comment: 30 pages, to appear in J Math Phy