Taxing Nonprofits out of Business

In the last twenty years, the number of nonprofit organizations has exploded; there are more than 1.2 million organizations registered with the Internal Revenue Service. Donations and government grants have decreased, while at the same time, nonprofits are facing increasing demands on their services. As a result, nonprofit organizations have been forced to devise new strategies for acquiring funds. Some nonprofit organizations have resorted to renting their mailing lists to businesses and other nonprofit organizations and have licensed their names and logos to be displayed on affinity credit cards offered by banks to consumers. Nonprofit organizations have argued that these funds are not subject to the unrelated business income tax and consider them to be exempt as royalties. The Internal Revenue Service, and initially the courts, disagreed. Revenue from these two sources should continue to be classified as royalty income. These royalties operate in a fashion analogous to traditional mineral rights royalties, which are exempt from the unrelated business income tax. Mineral rights royalties are divided into a taxable working interest, which bears the risks and benefits of the venture, and the exempt investment interest held by the nonprofit. These new royalties can be divided the same way into these two interests. In fact, it can be argued that this approach could be applied to other income items to determine if they should be exempt from the unrelated business income tax. Further, mailing list rentals and affinity credit card licenses do not contain even the potential to harm competition. However, taxing this income may well hinder certain nonprofits from functioning and discriminate in favor of older, more moneyed organizations

Is the United States Tax Court Exempt from Administrative Law Jurisprudence When Acting as a Reviewing Court

Commentators have argued that the Tax Court should fill in the gaps in its statutory authority for collection due process appeals by turning to traditional administrative law jurisprudence, including the APA, which suggestion the Tax Court has resisted despite the fact that the federal district court did so. The majority of the Tax Court insists that it has never been subject to administrative law jurisprudence or the APA, nor could it be. Most of the courts of appeals that have considered the issue have held that the Tax Court is bound by the APA and traditional administrative law jurisprudence when the Tax Court is acting as a reviewing court. An exploration of the Tax Court\u27s and the APA\u27s history reveals that the Tax Court can be, and should be, subject to the APA and traditional administrative law jurisprudence when it acts as a reviewing court of agency action

PHYSICOCHEMICAL CHARACTERIZATION OF MOUSE MYELOMA PROTEINS: DEMONSTRATION OF HETEROGENEITY FOR EACH MYELOMA GLOBULIN

Physicochemical characterization of mouse myeloma proteins revealed the individuality of each myeloma protein. When the myeloma proteins are considered collectively a wide range of individual properties were represented, including electrophoretic mobilities varying from the gamma to alpha region, hexose contents from 1 to 4 per cent, and ultracentrifugal components from 6.5 to 13 S. The 20 myeloma proteins could be divided into groups, the gamma type and the beta type myeloma globulins, on the basis of physicochemical, as well as immunoelectrophoretic, studies. Two gamma type myeloma proteins (5563, MPC-11) resembled normal gamma globulins, sedimenting as a single 6.5 S peak in the ultracentrifuge, and having a relatively low hexose content (1 per cent). Eighteen beta type mouse myeloma proteins differed from gamma myeloma proteins and, typically, were found on ultracentrifugal analysis to have multiple components with sedimentation coefficients of 6.5, 9, 11, and 13 S, having a higher hexose content (2 to 4 per cent) as well as distinctive chromatographic and starch gel electrophoretic properties. All of the mouse myeloma proteins were heterogeneous and heterogeneity of two types was observed. Polymer formation was responsible for the 9, 11, and/or 13 S components seen on ultracentrifugation of the beta type myeloma proteins. Starch gel electrophoresis revealed this type of heterogeneity as relatively widely separated myeloma protein components, presumably owing to the retardation effect of starch gel on the electrophoretic migration of the larger polymers. Starch gel electrophoresis revealed a different type of heterogeneity for the two gamma type myeloma proteins, each of these being shown to contain 5 or more components differing only in electrophoretic properties. The physicochemical characteristics of the γ-type and β-type myeloma proteins in the mouse indicated the close similarity of these proteins to the γ- and β-2A-myeloma proteins in man

The evolution of glutathione metabolism in phototrophic microorganisms

The low molecular weight thiol composition of a variety of phototropic microorganisms is examined in order to ascertain how evolution of glutathione (GSH) production is related to the evolution of oxygenic photosynthesis. Cells were extracted in the presence of monobromobimane (mBBr) to convert thiols (RSH) to fluorescent derivatives (RSmB) which were analyzed by high performance liquid chromatography (HPLC). Significant levels of GSH were not found in green sulfur bacteria. Substantial levels were present in purple bacteria, cyanobacteria, and eukaryotic algae. Other thiols measured included cysteine, gamma-glutamylcysteine, thiosulfate, coenzyme A, and sulfide. Many of the organisms also exhibited a marked ability to reduce mBBr to syn-(methyl,methyl)bimane, an ability which was quenched by treatment with 2-pyridyl disulfide or 5,5 prime-bisdithio - (2-nitrobenzoic acid) prior to reaction with mBBr. These observations indicate the presence of a reducing system capable of electron transfer to mBBr and reduction of reactive disulfides. The distribution of GSH in phototropic eubacteria indicates that GSH synthesis evolved at or around the time that oxygenic photosynthesis evolved

Self-monitoring for improving control of blood pressue in patients with hypertension

The objective of this review is to determine the effect of SBPM in adults with hypertension on blood pressure control as compared to OBPM or usual care

THE IMMUNOGLOBULINS OF MICE : V. THE METABOLIC (CATABOLIC) PROPERTIES OF FIVE IMMUNOGLOBULIN CLASSES

The metabolic properties of immunoglobulin were investigated by comparing five classes of mouse immunoglobulin. Three forms of 7S immunoglobulin had different rates of catabolism. The fractional rates of catabolism were found to be about 13 per cent per day for 7S γ2a-globulin; 25 per cent for 7S γ2b-globulin; and 17 per cent for 7S γ1-globulin. Catabolism of the three classes of 7S γ-globulin (γ2a, γ2b, and γ1) were prolonged at low serum 7S γ-globulin levels and accelerated at high serum 7S γ-globulin levels. Each of the 7S γ-globulin components was influenced by the serum level of the other mouse 7S γ-globulin components and by exogenously administered human 7S γ-globulin. They were not appreciably altered, however, by the serum level of IgA (γ1A-, β2A-globulin). The progressively changing (longer) half-times observed in turnover studies of normal IgG (7S γ-globulin) may be caused by catabolic heterogeneity of normal 7S immunoglobulins which are immunochemically and catabolically related to γ2a-, γ2b-, and 7S γ1-myeloma proteins. These studies indicate that the 7S γ2a-, 7S γ2b-, and 7S γ1-globulins share a common catabolic control mechanism. This mechanism is influenced by the serum level of each of these components, but is independent of the serum level of IgA (γ1A-globulin) and probably is independent of IgM (γ1M-globulin). Catabolism of IgA (γ1A-, β2A-globulin) and IgM (γ1M-globulin) was much more rapid than the catabolism of the 7S γ-globulins. The halftimes of the IgA and IgM were approximately 1.2 and 0.5 days respectively. The fractional rate of catabolism of IgA and IgM seemed to be independent of their serum concentration. The rate of catabolism, as well as the rate of synthesis, was shown to play a major role in determining the serum level of each class of immunoglobulin

ENZYMATICALLY PRODUCED SUBUNITS OF PROTEINS FORMED BY PLASMA CELLS IN MICE : II. β2A-MYELOMA PROTEIN AND BENCE JONES PROTEIN

The relationship of Bence Jones protein (mol wt = 45,000) to a β2A-myeloma protein (mol wt = 160,000) formed by the same mouse plasma cell tumor (MPC-2) was investigated. The β2A-myeloma protein was split by treatment with papain and cysteine into fragments (S20,w = 3.7S), similar in size to the Bence Jones protein (S20,w = 3.6S). Two types of fragments with distinct antigenic groupings designated S and F, were present in the MPC-2 myeloma protein digest. These were partially separated by DEAE-cellulose chromatography. The Bence Jones protein was found to share antigenic determinants with S fragments from the MPC-2 β2A-myeloma protein and with S fragments from γ-globulins. Physicochemical observations indicated, however, that the Bence Jones protein was not identical to the globulin fragments produced by treatment with papain and cysteine. Comparison of the S and F fragments from β2A- and γ-globulins revealed that the antigenic features shared by the various globulins derived from plasma cells (γ- and β2A-myeloma proteins, the range of normal γ-globulins) are largely properties of the S fragments, whereas the distinctive antigenic differences between the γ- and β2A-myeloma proteins were properties which appeared in the F fragments of the molecules