Effect of Light and Benzyladenine on Dark-Treated Growing Rice (Oryza sativa) Leaves II. Changes in Peroxidase Activity

Changes in peroxidase activity were studied in the attachedfirst leaf of dark-treated Oryza sativa L. cv. Bala seedlingsin response to benzyladenine and light treatments during laterperiods of leaf growth, prior to maturation. Darkness causeda mild decrease in peroxidase activity; but in illuminated leaves,the enzyme activity was stable at all times. There was a sharprise in peroxidase activity in dark-treated leaves upon lightor benzyladenine application, irrespective of the time of treatment.Benzyladenine treatment to illuminated leaves also caused arise in peroxidase activity. Exogenous hydrogen peroxide, glycolateand amizol resulted in a rise in peroxidase activity, whichwas further enhanced by benzyladenine treatment in both lightand dark incubated leaves. Proline maintained chlorophyll levels,whereas hydroxyproline caused chlorophyll degradation. Benzyladenineenhanced the proline effect and counteracted the hydroxyprolineeffect on chlorophyll. Both proline and hydroxyproline increasedperoxidase activity in the leaves of light and dark incubatedseedlings, and the enzyme activity further increased after benzyladeninetreatment. (Received December 7, 1984; Accepted May 8, 1985)     

Distribution of N,P, K,Ca, Mg,S, Zn,Fe, Mn and Cu in groundnut

Summary Concentration of N, P, K, Ca, Mg and S in summer groundnut crop was higher than in kharif while Zn, Fe, Mn and Cu contents were higher in summer crop. Kernel's N, P and Zn; Leaflet's Ca and Mn; Stem's K and Fe; Root's S and Cu and Petiole's Mg contents were highest. Shell's N, P, K, Mg, S, Zn and Cu; Kernel's Ca, Fe and Mn contents were the least. N, P, K, S, Zn and Cu concentrations decreased linearly as the crop grew. Ca, Mg, Fe and Mn concentrations did not display any distinct pattern. Ca concentration was positively correlated with pod yield in both the seasons.     

HTLV-III env gene products synthesized in E. coli are recognized by antibodies present in the sera of AIDS patients

The envelope gene of HTLV-III, the retrovirus directly linked to AIDS, encodes a protein of 856 amino acids. Our sequence analysis of the cloned HTLV-III (HXB-3) env gene and its comparison with other isolates reveal significant divergence, especially in the external portion of this protein. A large segment of the env gene (1800 bp) was inserted into the expression vector pEV-vrf3, and a corresponding 68 kd protein, which encompasses both the extracellular and the membrane-associated regions of the native protein, was produced in E. coli. Several smaller polypeptides, which appear to be internal initiation products, were also produced. All 50 AIDS patient sera obtained from different locations in the United States specifically recognized the bacterially synthesized envelope proteins, as judged by Western blots. This suggests that these proteins will be useful for the diagnosis of HTLV-III infection and possibly as a vaccine against AIDS.     

Phosphoethanolamine and phosphocholine transferases in gray matter and white matter from developing rat brain

We have studied the activities of 2′,3′-cyclic nucleotide 3′-phosphohydrolase, 1,2-diacylglycerol: CDPethanolamine phosphoethanolamine transferase (EC 2.7.8.1), and 1,2-diacylglycerol: CDPcholine phosphocholine transferase (EC 2.7.8.2) in developing rat brain gray matter and white matter. The specific activity of cyclic nucleotide phosphohydrolase was 5–8 fold higher in white matter than in gray matter at all ages. No significant changes were observed during development. The specific activity of phosphocholine transferase was 2 to 3 fold higher than phosphoethanolamine transferase at all ages both in gray and white matter. Both phosphocholine transferase and phosphoethanolamine transferase increased more than 2 fold in specific activity between 14 and 90 days of age. The total activity of phosphocholine transferase also showed an increase during development. The apparentK _m values for nucleotides and dicaprin were similar in gray matter and white matter. Except for lowK _m values for nucleotides at 14 days of age, no significant changes were observed during development. Changes in rates of glycerophospholipid synthesis may be partly due to the specific activities of these enzymes but are also determined by the quantities of substrates and inhibitors and by affinities for the substrates. Special Issue dedicated to Dr. Eugene Kreps.     

Long-chain acyl CoA synthetase in microsomes from rat brain gray matter and white matter

Long-chain acyl coenzyme A (CoA) synthetase in homogenates and microsomes from rat brain gray and white matter was studied. The formation of the thioesters of CoA was studied upon addition of [1-¹⁴C]-labeled fatty acids. The maximal activities were seen with linoleic acid, followed by arachidonic, palmitic, and docosahexaenoic acids in both gray and white matter homogenates and microsomes. The specific activities in microsomes were 3–5 times higher than in homogenates. The presence of Triton X-100 in the assay system enhanced the activity of long-chain acyl CoA synthetase in homogenates. The effect was more pronounced in palmitic and docosahexaenoic acid activation. The apparentK _m values andV _max values for palmitic and docosahexaenoic acids were much lower than for linoleic and arachidonic acids. The presence of Triton X-100 in the medium caused a definite decrease in the apparentK _m and Vmax values for all the fatty acid except palmitic acid in which case the reverse was true. There were no significant differences observed in the kinetic measurements between gray and white matter microsomes. These findings are similar to those resulting from the known interference of Triton X-100 in the measurement of kinetic variables of long-chain acyl CoA synthetase of liver microsomes. In this work, no correlation was observed between the fatty acid composition of gray and white matter and the capacity of these tissues for the activation of different fatty acids.     

The nucleotide sequence of a rat liver glutathione S-transferase subunit cDNA clone

We have determined the nucleotide sequence of a cloned cDNA derived from liver poly(A) RNA of pentobarbital-treated rats encoding a glutathione S-transferase subunit. This cDNA clone pGTR261 contains one open reading frame of 222 amino acids, a complete 3' noncoding region, and 63 nucleotides in the 5' noncoding region. The cloned DNA hybridizes to rat poly(A) RNA in a tissue-specific fashion, with strong signals to liver and kidney poly(A) RNA(s) of approximately 1100 and approximately 1400 nucleotides in size but little or no hybridization to poly(A) RNAs from heart, lung, seminal vesicles, spleen, or testis under stringent conditions. Our sequence covers the cDNA sequence of pGST94 which contains a partial coding sequence for a liver glutathione S-transferase subunit of Ya size. Comparison of sequences with our earlier clone pGTR112 suggests that there are at least two mRNA species coding for two different subunits of the Ya (Mr = 25,600) subunit family with very limited amino acid substitutions mainly of conserved polarity. The divergent 3' noncoding sequences should be useful molecular probes in differentiating these two different but otherwise very similar subunits in induction and genomic structure analyses. Our results suggest that tissue-specific expression of the glutathione S-transferase subunits represented by the sequences of pGTR261 and pGTR112 may occur at or prior to the level of RNA processing.