A new and distinctive male-sterile,female-fertile desynaptic mutant in soybean (Glycine max)

A spontaneous desynaptic mutation, affecting only microsporogenesis and causing pollen sterility, has been detected in BR97-12986H, a line of the official Brazilian soybean breeding program. In this male-sterile, female-fertile mutant, up to metaphase II, the meiotic behavior was similar to that described for the st series of synaptic mutants previously reported in soybean. Besides many univalents, few or total absence of bivalents were recorded in diakinesis. Bivalents presented one or two terminal chiasmata, while univalents retained the sister chromatid cohesion. Bivalents and most univalents congregated at the equatorial metaphase plate, although univalents frequently migrated to the poles prematurely. Laggards resulting from delay in chiasmata terminalization were also recorded. Distinctly different in their behavior from st series soybean mutants, telophase I-originated micronuclei of different sizes organized their own spindle in the second division. This behavior contributed towards an increase in genome fractionation. Several microspores and microcytes of different sizes were recorded at the end of meiosis. Pollen sterility was estimated at 91.2%. Segregation ratio for sterility in this line and its progenies reached 3:1. Allelism tests with st series of synaptic mutants are in progress. The importance of male-sterile, female-fertile mutations for soybean breeding programs is discussed.     

A study on the pretreatment of a sugarcane bagasse sample with dilute sulfuric acid

Experiments based on a 2³ central composite full factorial design were carried out in 200-ml stainless-steel containers to study the pretreatment, with dilute sulfuric acid, of a sugarcane bagasse sample obtained from a local sugar–alcohol mill. The independent variables selected for study were temperature, varied from 112.5°C to 157.5°C, residence time, varied from 5.0 to 35.0 min, and sulfuric acid concentration, varied from 0.0% to 3.0% (w/v). Bagasse loading of 15% (w/w) was used in all experiments. Statistical analysis of the experimental results showed that all three independent variables significantly influenced the response variables, namely the bagasse solubilization, efficiency of xylose recovery in the hemicellulosic hydrolysate, efficiency of cellulose enzymatic saccharification, and percentages of cellulose, hemicellulose, and lignin in the pretreated solids. Temperature was the factor that influenced the response variables the most, followed by acid concentration and residence time, in that order. Although harsher pretreatment conditions promoted almost complete removal of the hemicellulosic fraction, the amount of xylose recovered in the hemicellulosic hydrolysate did not exceed 61.8% of the maximum theoretical value. Cellulose enzymatic saccharification was favored by more efficient removal of hemicellulose during the pretreatment. However, detoxification of the hemicellulosic hydrolysate was necessary for better bioconversion of the sugars to ethanol.     

Variation in sensitivity of the cardiac glycoside receptor characteristics of (Na+ + K+)-ATPase to lipolysis and temperature.

1. The rate of binding of [3H]ouabain to untreated membrane preparations of [Na+ +K+]-ATPase is a timperature--dependent process displaying a thermal transition close to 25degreesC. The apparent energies of activation which can be calculated above and below this transition are similar to, but not identical with, those previously reported for activation of the enzyme by cations. 2. Treatment of the enzyme preparation with detergents or lipolysis with phospholipase A eliminates the thermal transition resulting in linear Arrhenius plots. 3. The number of sites available for [3H]ouabain binding is not temperature dependent as the amount of [3H]ouabain bound at equillbrium is not changed between 10 and 37 degrees C. 4. Treatment of the enzyme with phospholipase A results in time-dependent changes in the number of binding sites for [3H]ouabain at equilibrium. 5. Treatment of the membrane enzyme preparations with detergents reveals additional [3H]ouabain binding sites which are extremely sensitive to lipolysis with phospholipase A. 6. There are a number of [3H]ouabain binding sites which remain resistant to lipolysis by phospholipase A in either untreated or detergent-treated membrane preparations. 7. It is suggested that [3H]ouabain binding sites exist in the membrane in at least two different environments, one of which is resistant the other sensitive to attack by phopholipase A.