Ventricular septal defect with bidirectional shunting: Mathematical considerations

Previously proposed formulae for the quantitative estimation of bidirectional shunts across ventricular septal defects require determination of the oxygen contents of mixed venous, pulmonary artery, pulmonary venous, and aortic blood. Because these formulae do not take into account the mixing of oxygenated with unoxygenated blood within the ventricles, their use must result in underestimation of shunt flows in each direction. A mathematical model for a ventricular defect is examined, in which it is assumed that mixing of blood occurs in each of six sites in the venae cavae or right atrium, right ventricle, pulmonary artery, left atrium, left ventricle, and aorta. A total of fourteen streams of blood can flow from one to another of these mixing sites. As long as complete mixing occurs in the six specified mixing sites, any degree of mixing or non-mixing of the various streams is permitted. From the equations characterizing the model, formulae are derived in which the shunt flow in each direction is expressed in terms of the oxygen contents in the six mixing sites and the fractions of blood which enter the shunt from either side without prior mixing in a ventricular mixing site. The previously reported formulae, which apply when no ventricular mixing is allowed to occur, lead to theoretical minimum values for the shunt flows in each direction. At the opposite extreme where all the shunting blood is required to mix in a ventricle before entering the shunt, formulae for maximum possible shunt flows are also obtained. The absolute values for the left-to-right and right-to-left shunt flows, which must lie somewhere between the theoretical maximum and minimum values, cannot be computed from blood gas data alone. This work was supported in part by grant HE-07563 from the National Heart Institute of the National Institutes of Health and grants-in-aid from the American and North Carolina Heart Associations and the Life Insurance Medical Research Fund. Work completed during tenure as U.S.P.H.S. post-doctoral fellow.     

Identification of Fluorescent-Antibody Labeled Group A Streptococci by Fluorometry

A quantitative system, amenable to automation, for determining the presence of group A streptococci in broth culture is described. After separation from the broth, the cells' protein coats are removed by digestion with 0.1% trypsin, and they are then stained with anti-A fluorescent antibody (FA). Excess FA is removed, and bound FA is put into solution by dissociation with demineralized distilled water. The amount of FA bound to the cells is quantitated by fluorometry of the solution. The level of nonspecific staining is measured by staining the cells with fluorescein-conjugated normal rabbit globulin absorbed with group A cells, dissociating, and quantifying, as above. The two quantities are subtracted to measure specific binding of FA to group A cells. A clinical trial showed 92% agreement with microscopists.     

Prostaglandin F-2 alpha causes regression of an hCG-induced corpus luteum before day 5 of its lifespan in cattle

The experimental objective was to evaluate how a spontaneously formed corpus luteum (CL) differed in its response to prostaglandin (PG) F-2 alpha, given during the first 5 days after ovulation, from a CL induced during dioestrus with hCG. Sixteen Holstein heifers were used during each of 2 consecutive oestrous cycles. During the first cycle (sham cycle), heifers were given no PGF-2 alpha (control) or PGF-2 alpha (25 mg, i.m.) on Day 2, 4 or 6 (oestrus = Day 0). During the second cycle (hCG-treated cycle), heifers were given hCG (5000 i.u., i.m.) on Day 10, followed by no PGF-2 alpha (control) or PGF-2 alpha on Day 12, 14 or 16, corresponding to 2, 4 or 6 days after the ovulatory dose of hCG. A new ovulation was induced in 13 of 16 heifers given hCG on Day 10. Luteolysis did not occur immediately in heifers given PGF-2 alpha on Day 2 or 4 during the sham cycle, but concentration of progesterone in serum during the remainder of the cycle was lower in heifers given PGF-2 alpha on Day 4 than in sham controls or heifers given PGF-2 alpha on Day 2 (P less than 0.05). Luteolysis occurred immediately in heifers given PGF-2 alpha on Day 6 of the sham cycle or on Day 12, 14 or 16 of the hCG-treated cycle, with concentration of progesterone in serum decreasing to less than 1 ng/ml within 2 days.(ABSTRACT TRUNCATED AT 250 WORDS)     

Kinetics of MgATP-dependent iron chelation from the Fe-protein of the Azotobacter vinelandii nitrogenase complex. Evidence for two states

Chelation of Fe from the Fe-protein component (Av2) of Azotobacter vinelandii nitrogenase has been investigated. The chelation, which requires MgATP binding by Av2, is best described as a two-exponential process. The rates for the two phases differed by approximately 10-fold and increased as the concentration of MgATP was increased. The rates for both phases were 50% of maximum at approximately 1.5 mM MgATP. At MgATP concentrations greater than 100 microM, the more rapid phase represented approximately 25% of the total Fe chelated from Av2. However, below 100 microM MgATP, the proportion of the faster phase decreased until at 20 microM MgATP, only a single phase could be detected. The properties of Av2 were studied at various stages of Fe chelation. The partially chelated protein was isolated from the reaction by gel filtration and was subjected to a second MgATP-dependent Fe chelation. Material isolated after the completion of the first phase regained biphasic kinetics in subsequent chelation reactions. However, if MgATP was present during the isolation of Av2, then only a single phase was observed in the subsequent chelation studies. In addition, the enzymatic activity of Av2 decreased concomitantly with total Fe chelation. To account for these observations, a model is presented in which Av2 exists in two conformers. Fe chelation is proposed to occur from either conformer but only when two MgATP are bound. Both conformers bind MgATP with the same affinity but are distinguished by a 10-fold difference in chelation rate. The two conformers are in equilibrium and can interconvert only in the absence of MgATP. That is, MgATP binding prevents the conversion of the two conformational states.