Use of leaf meters to provide an instantaneous assessment of leaf chlorophyll has become common, but calibration of meter output into direct units of leaf chlorophyll concentration has been difficult and an understanding of the relationship between these two parameters has remained elusive. We examined the correlation of soybean (Glycine max) and maize (Zea mays L.) leaf chlorophyll concentration, as measured by organic extraction and spectrophotometric analysis, with output (M) of the Minolta SPAD-502 leaf chlorophyll meter. The relationship is non-linear and can be described by the equation chlorophyll (μmol m(-2))=10((M0.265)), r (2)=0.94. Use of such an exponential equation is theoretically justified and forces a more appropriate fit to a limited data set than polynomial equations. The exact relationship will vary from meter to meter, but will be similar and can be readily determined by empirical methods. The ability to rapidly determine leaf chlorophyll concentrations by use of the calibration method reported herein should be useful in studies on photosynthesis and crop physiology.

Soybean [Glycine max (L.) Merr.] yield, when regressed on water needed to replenish 0 to 100% seasonal evapotranspiration (ET), generates an estimate of season‐specific water‐use efficiency (WUE). The impact of unpredictable water deficits might be lessened if high‐yielding genotypes had a smaller beta. Our objective was to determine the genetic basis of beta and carbon isotope discrimination (CID), a theorized indicator of transpiration efficiency (TE). A ‘Minsoy’ × ‘Noir 1’ population of 236 recombinant inbred lines (RILs), genotyped at 665 loci, was evaluated in six water treatments (100, 80, 60, 40, 20, and 0% ET) for 2 yr. Water stress was mild in 1994, but high temperatures and no rainfall in 1995 led to a drought so severe that the 100% ET treatment required 41 cm of irrigation. The 1995 yield‐to‐water regression was highly linear (28 kg ha−1 cm−1). Genotype × water (G × W) interaction was due to genotypic heterogeneity in beta The CID vs. beta correlation was low (r = 0.26), so selection for better leaf TE may not improve crop WUE. Selection of low beta (less sensitivity to drought) will be difficult, given the yield beta vs. yield correlation (r = 0.71). The major quantitative trait loci (QTL) for yield beta, yield, and CID were coincident with maturity and/or determinancy QTLs, except for a CID QTL in linkage group U09‐C2, but it had no effect on beta Genetic improvement of soybean yield performance under drought would be better achieved by coupling a high‐yield grand mean with a high‐ (not low‐) yield beta

Biochemical analysis of proteins relies on accurate quantitation of protein concentration. This unit describes how to perform commonly used protein assays, e.g., Lowry, Bradford, BCA, and UV spectroscopic protein assays. The primary focus of the unit is assay selection, emphasizing sample and buffer compatibility. Protein assay standard curves and data processing fundamentals are discussed in detail. This unit also details high-throughput adaptations of the commonly used protein assays, and also contains a protocol for BCA assay of total protein in SDS-PAGE sample buffer that is used for equal loading of SDS-PAGE gels, which is reliable, inexpensive, and quick.

Background: The identification of IgE epitopes for proteins is the first step in understanding the interaction of allergens with the immune system. Proteins from the legume family have shown in vitro cross-reactivity in IgE-binding assays, but this cross-reactivity is rarely clinically significant. Resolution of this discrepancy requires IgE epitope mapping of legume family protein allergens. Methods: We constructed six fusion proteins representing overlapping regions of soybean glycinin G1 acidic chain. These fusion proteins were used in immunoblotting and a novel sandwich ELISA with pooled sera from soy-allergic individuals to reveal a common IgE-binding region. This region was the focus for IgE epitope mapping using overlapping synthetic peptides. Results: Data from the fusion protein experiments revealed an IgE-binding region consisting of residues F192–I265. Analysis of the overlapping synthetic peptides to this region indicated that IgE epitopes to glycinin G1 acidic chain consist of residues G217–V235 and G253–I265. The epitopes identified for glycinin G1 acidic chain are homologous to IgE epitopes previously identified for the peanut allergen Ara h 3 [1]. However, residues identified by alanine scanning in the peanut epitopes as being important for IgE binding are different in the natural soybean epitopes. Conclusions: The IgE epitopes identified for glycinin G1 acidic chain apparently represent an allergenic region of several legume family seed storage proteins. Our findings indicate that the identification of IgE epitopes and structural analysis of legume family proteins will provide valuable information to the study of food allergies.

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