Metabolism of n-Butane and 2-Butanone by Mycobacterium vaccae

n-Butane was metabolized in Mycobacterium vaccae (JOB5) via terminal oxidation. This organism metabolized 2-butanone through propionate (or propionyl coenzyme A). Subterminal oxidation in M. vaccae was apparently limited to propane.     

Binding of Streptococcal Competence Factor by the Spheroplast Membrane of a Group H Streptococcus

The binding of streptococcal competence factor (CF) was found to be specific for a strain of streptococcus which was capable of undergoing competence induction. Three other streptococcal strains which could not be induced to competence, did not bind CF. CF binding was independent of time, temperature, age of the culture, and type of growth media employed. Several observations indicated that the receptor sites for CF are located in the bacterial membrane: (i) the retention of CF by spheroplasts, (ii) the binding of CF by isolated membrane fractions, and (iii), the degradation of CF binding capacity of membranes by different chemicals and enzymes.     

Male and female meiosis in grasshoppers

Male meiosis in the grasshopper Stethophyma grossum is well known as an example of proximal chiasma localisation. An investigation of female meiosis in oocytes of this species shows that both the frequency and distribution of chiasmata are quite different from the male situation. Mean chiasma frequency per cell (14.98) in considerably higher in females than in males (11.28) which agrees with the trend established in other comparative studies of male and female meiosis. More strikingly, males and females also show not only different but quite opposite patterns of chiasma distribution. In spermatocytes of males, chiasmata are strictly localised proximally in most bivalents, but in oocytes of females very few chiasmata form in proximal regions and nearly all chiasmata form either in distal or interstitial regions. The genetical significance of these findings is considered.     

Divergent Metabolic Pathways for Propane and Propionate Utilization by a Soil Isolate

The metabolism of propane and propionate by a soil isolate (Brevibacterium sp. strain JOB5) was investigated. The presence of isocitrate lyase in cells grown on isopropanol, acetate, or propane and the absence of this inducible enzyme in n-propanol- and propionate-grown cells suggested that propane is not metabolized via C-terminal oxidation. Methylmalonyl coenzyme A mutase and malate synthase are constitutive in this organism. The incorporation of ¹⁴CO₂ into pyruvate accumulated during propionate utilization suggests that propionate is metabolized via the methyl-malonyl-succinate pathway. These results were further substantiated by radiorespirometric studies with propionate-1-¹⁴C, -2-¹⁴C, and -3-¹⁴C as substrate. Propane -2-¹⁴C was shown, by unlabeled competitor experiments, to be oxidized to acetone; acetone and isopropanol are oxidized in this organism to acetol. Cleavage of acetol to acetate and CO₂ would yield the inducer for the isocitrate lyase present in propane-grown cells.     

Effect of Substrate on the Fatty Acid Composition of Hydrocarbon-utilizing Microorganisms

The fatty acid pattern in three hydrocarbon-utilizing bacteria during growth on various substrates was examined. The predominant fatty acids in acetate-grown cells were C(16), C(16:1), C(18:1), and Br-C(19) and the major fatty acids in propane-grown cells were C(15), C(17), C(17:1), C(18:1), and Br-C(18). When one organism (Mycobacterium sp. strain OFS) was grown on the n-alkanes from C(13) to C(17), the major fatty acid in the cells was of the same chain length as the substrate. Studies on the incorporation of acetate into the cellular fatty acids of microorganisms growing on C(15) and C(17)n-alkanes suggest that the oxidative products of the substrate are incorporated into the cellular fatty acids without degradation to acetate.     

A protein factor inhibiting the magnesium-activated adenosine triphosphatase of desensitized-actomyosin

1. The preparation and properties of a myofibrillar protein factor which inhibits the Mg(2+)-activated adenosine triphosphatase of desensitized actomyosin is described. 2. This factor had negligible effect on the Mg(2+)-activated adenosine triphosphatase of natural actomyosin and on the Ca(2+)-activated adenosine triphosphatases of desensitized actomyosin and myosin. 3. The Mg(2+)-activated inosine triphosphatase activity of desensitized actomyosin was not affected by the factor. 4. The inhibitory effect was sensitive to ionic strength. In addition to their ionic effects Mg(2+) and Ca(2+) appeared to have a specific action in reducing the effect of the inhibitor. 5. F-actin reduced the inhibition whereas Bailey-type tropo-myosin had little effect. 6. As far as can be judged from the reported experiments this factor is different from any of the previously described myofibrillar components.