Root to shoot ratio of crops as influenced by CO2

Crops of tomorrow are likely to grow under higher levels of atmospheric CO₂. Fundamental crop growth processes will be affected and chief among these is carbon allocation. The root to shoot ratio (R:S, defined as dry weight of root biomass divided by dry weight of shoot biomass) depends upon the partitioning of photosynthate which may be influenced by environmental stimuli. Exposure of plant canopies to high CO₂ concentration often stimulates the growth of both shoot and root, but the question remains whether elevated atmospheric CO₂ concentration will affect roots and shoots of crop plants proportionally. Since elevated CO₂ can induce changes in plant structure and function, there may be differences in allocation between root and shoot, at least under some conditions. The effect of elevated atmospheric CO₂ on carbon allocation has yet to be fully elucidated, especially in the context of changing resource availability. Herein we review root to shoot allocation as affected by increased concentrations of atmospheric CO₂ and provide recommendations for further research. Review of the available literature shows substantial variation in R:S response for crop plants. In many cases (59.5%) R:S increased, in a very few (3.0%) remained unchanged, and in others (37.5%) decreased. The explanation for these differences probably resides in crop type, resource supply, and other experimental factors. Efforts to understand allocation under CO₂ enrichment will add substantially to the global change response data base.Abbreviations R:S root to shoot ratio, dry weight basis     

Therapeutic application of various immunostimulators on the L2C guinea-pig leukemia

Summary Immunostimulators such as Corynebacterium parvum (C. parvum), Bacillus Calmette-Guerin (BCG), pyran copolymer, and glucan were examined in the guinea pig L ₂ C lymphoblastic leukemia model to determine their capacity for therapeutic modulation of the immune response of the host toward controlling leukemic cell proliferation. The dose, route, and frequency of administration of the stimulators were also evaluated as a function of time in order to obtain an optimal antileukemic effect. Results indicated that only C. parvum and BCG were capable of significantly increasing host survival when given 1 day after an inoculation of 1.5×10 ⁴ viable leukemic cells. Administration of BCG or C. parvum, alone or in combination with irradiated blast cells on either days 4 or 7, was totally ineffective in prolonging survival. In the majority of cases, enhanced leukemic growth was observed on these days. The combination of BCG and/or C. parvum with irradiated syngeneic blast cells given 24 h after leukemia inoculation promoted a synergistic response with a significant increase in median survival time and a number of long-term survivors.This work was supported by contract N01-CP-53566 within the Virus Cancer Program of the National Cancer Institute     

A one tube flow problem arising in physiology

A mathematical analysis, including existence and uniqueness, is given for some boundary value problems which model the flow of a fluid-solute mixture in a tube which is placed in an interstitium. The model permits an interchange of fluid and solute across the tube walls.     

A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the Escherichia coli lactose operon regulatory system.

The use of gel electrophoresis for quantitative studies of DNA-protein interactions is described. This rapid and simple technique involves separation of free DNA from DNA-protein complexes based on differences in their electrophoretic mobilities in polyacrylamide gels. Under favorable conditions both unbound DNA and DNA associated with protein can be quantified. This gel method is applied to the study of the E. coli lactose operon regulatory system. At ionic strengths in the physiological range, the catabolite activator protein (CAP) is shown to form a long-lived complex with the wild type lac promotor, but not with a CAP-insensitive mutant. Formation of a stable "open" or "melted-in" complex of RNA polymerase with the wild type promoter requires the participation of CAP and cyclic AMP. Further, it is demonstrated that even when pre-formed in the presence of CAP-cAMP, the polymerase-promoter open complex becomes unstable if CAP is then selectively removed.     

Isolation and characterization of the 160,000-Da phosphotyrosyl protein, a putative participant in insulin signaling.

The 160,000-Da protein (pp 160) which is rapidly phosphorylated on tyrosine in response to insulin and thus is a putative participant in signaling from the insulin receptor has been purified to homogeneity from 3T3-L1 adipocytes. Isolation of this protein was accomplished by chromatography on an immobilized monoclonal antibody against phosphotyrosine, followed by gel electrophoresis. Sufficient protein was obtained to allow the determination of the sequences of several peptides, which in turn enabled the development of anti-peptide antibodies that specifically recognize pp 160. Immunoblotting of 3T3-L1 adipocyte lysates, together with the purified pp 160 as a standard, indicate that an insulin-treated 3T3-L1 adipocyte possesses about 230,000 copies of tyrosine-phosphorylated pp160 and that this amount is approximately 25% of the total pp160 in the cell. The number of tyrosine-phosphorylated pp160s per cell is approximately the same as that of insulin receptor beta subunits. These results provide further evidence for a role of pp160 in insulin signaling. Moreover, the availability of purified protein and knowledge of peptide sequences will allow the elucidation of the structure and function of this protein.     

The association of insulin-elicited phosphotyrosine proteins with src homology 2 domains.

The interactions of the phosphotyrosine (Tyr(P))-containing proteins in basal and insulin-stimulated 3T3-L1 adipocytes with src homology 2 (SH2) domains from phosphatidylinositol 3-kinase (PI3K), ras GTPase-activating protein (GAP), and phospholipase C gamma have been examined. The Tyr(P) forms of the insulin receptor and its 160-kDa substrate protein (pp160) associated with fusion proteins containing either or both the SH2 domains of PI3K, but not with fusion proteins containing the two SH2 domains of GAP or phospholipase C gamma. These results demonstrate a specificity for the association of the Tyr(P) form of the insulin receptor and pp160 with SH2 domains that parallels the reported effects of insulin on PI3K, GAP, and phospholipase C gamma in vivo. Immunoprecipitates of pp160 from the cytosol of insulin-treated, but not basal, 3T3-L1 adipocytes contained PI3K activity. Moreover, the Tyr(P) form of pp160 with associated PI3K activity migrated at 10 S on a sucrose velocity gradient, whereas the Tyr(P) form without associated activity migrated at 6 S. These findings indicate that the Tyr(P) form of pp160 associates directly with PI3K in vivo.