Investigations on Simarouba glauca Dc. in El Salvador

The use of the kernels of Simarouba glauca as a potential source of vegetable oil was first noted in 1939. These kernels produce 62 per cent edible oil under commercial extraction procedures. The trees are polygamo-dioecious, thus creating a selection problem for commercial plantings. A progress report of investigations on the botany, propagation, selection, insect pests, and diseases is given.

     

Palm Chromosome Studies Facilitated by Pollen Culture on a Colchicine-Lactose Medium

This technique is very useful where pollen is readily available and when roots or microspore mother cells are difficult to obtain or to process. It provides a relatively uniform means of studying chromosomes in a great number of species. Pollen is collected from buds at anthesis or the day before and sown on a medium containing H₃BO₃, 100 ppm; colchicine, 0.04%; lactose, 12%; gelatin, 5%; egg albumen, 1 drop in 10 ml. The gametic chromosome complement is studied at mitosis of the generative cell in the pollen tube. In species which have sufficiently large chromosomes it is possible to construct idiograms for comparative studies. All palm species here reported have a haploid complement of n = 18, and the chromosomes range in length from 0.5-3.5 μ.     

Structure and function of the head in flabelligerid polychaetes

The functional anatomy of the head of Flabelliderma commensalis is described and compared to other flabelligerid polychaetes. Prostomial parts include the dorsal lip, the palps, two pairs of nuchal organs, four eyes and the prostomial lobe and ridge. The eyes are inverse pigment cup types with the medial portions of the sensory cells expanded to form a clear lens-like body. Peristomial parts include the median and ventral lips, the branchial membrane and the branchiae. The derivation of the nephridiopore is unknown. The spiraled branchiae of Coppingeria and the gill books of Diplocirrus are newly described variations in branchial structure. The head is retractable in some species and the anterior setigers are modified to form a protective setal cage. Two methods are employed for feeding: one for host fecal pellets and the other for detrital materials. Chemoreception, respiration, feeding and cleaning rely on a complex pattern of ciliary currents.     

Bifunctional indole-3-acetyl transferase catalyses synthesis and hydrolysis of indole-3-acetyl-myo-inositol in immature endosperm of Zea mays

1- O -(indole-3-acetyl)- β - d -glucose: myo -inositol indoleacetyl transferase (IA- myo -inositol synthase) is an important enzyme in IAA metabolism. This enzyme catalyses the transfer of the indole acetyl (IA) moiety from 1- O -(indole-3-acetyl)- β - d -glucose to myo -inositol to form IA- myo- inositol and glucose. IA- myo -inositol synthase was purified to an electrophoretically homogenous state from maize liquid endosperm by fractionation with ammonium sulphate, anion-exchange, adsorption on hydroxylapatite, affinity chromatography on ConA-Sepharose, preparative PAGE and isoelectric focusing. We thus obtained two enzyme preparations which differ in their R _f on 8% polyacrylamide gel. The preparation of R _f 0.36 contained a single 56.4 kDa polypeptide, whereas the preparation of R _f 0.39 consisted of two polypeptides of 56.4 and 53.5 kDa. Both purified preparations of IAInos synthase also exhibited the activity of an IAInos hydrolase, showing that the dual activity was associated with a single protein. Results of gel filtration and analytical SDS-PAGE suggest that the native enzyme exists as both a monomeric (65 kDa) and homo- or heterodimeric form (110–130 kDa). Analysis of peptide maps and amino acid sequences of two 21 amino-acid peptides showed that polypeptides of 56.4 and 53.5 kDa have the same primary structure and that the 3 kDa difference in molecular mass is probably caused by different glycosylation levels. Comparison of this partial and internal amino acid sequence with sequences of other plant acyltransferases indicated similarity to several proteins which belonged to the serine carboxypeptidase-like (SCPL) acyltransferase family.