A lipase inhibitor monoterpene and monoterpene glycosides from Monarda punctata

An 80% acetone extract of Monarda punctata showed an inhibitory effect on lipase activity in isolated mouse plasma in vitro and carvacrol was obtained as the active constituent. It had an IC₅₀ value of 4.07 mM in vitro and suppressed elevations in blood triacylglycerol levels in olive oil-loaded mice. Furthermore, from the whole plant, 22 compounds were isolated. Six monoterpene glycosides (3–8), a flavone glucuronide (9), and other known compounds were identified based on the results of spectroscopic analyses.     

拟美国薄荷的组织培养与快速繁殖

1植物名称拟美国薄荷(Monarda fistulosa Linn.)。2材料类别种子萌发的无菌苗。3培养条件种子萌发采用MS基本培养基。增殖培养基:(1)MS 6-BA 2.0 mg·L~(-1)(单位下同) NAA 0.1;(2)MS 6-BA 2.0 NAA 0.01;(3)MS 6-BA 3.0 NAA 0.01。壮苗培养基:(4)MS。生根培     

The pollination biology and breeding system of Monarda fistulosa (Labiatae)

Summary Successful cross-pollination of Monarda fistulosa is the result of a complex interaction among flower opening, the pollen-bearing areas of the pollinators and/or their behavior, and the maturation of the stigmas. The flowers open continuously from 0800–2000 h providing a temporally predictable rich source of nectar and pollen. Recently opened flowers may reduce the ability of bees to discriminate between resource rich and poor patches and encourage systematic foraging within patches. The continuous opening of flowers coupled with protandry also results in some flowers of most capitula being in the staminate and others in the pistillate phase. Autogamy is highly unlikely due to strong protandry and the spatial separation of anthers and stigmas. Geitonogamy, at least that mediated by Bombus is unlikely because the pollen is spread over a relatively large area of the wings, which reduces the likelihood of a stigma contacting just deposited pollen. Because pollen is transferred from the much smaller coxal area of Anthophora and other bees that mistake the stigmas of early pistillate phase flowers for stamens some geitonogamy seems inevitable. However, the delayed receptivity of young stigmas to self-pollen decreases the likelihood of self-pollen germinating on such stigmas. Older stigmas are equally receptive to self- and cross-pollen and the number of pollen grains germinating and pollen tubes reaching the base of the style increases with flower age.     

Monarda fistulosa hydrolate as antimicrobial agent in artificial media for the in vitro rearing of the tachinid parasitoid Exorista larvarum

Exorista larvarum (L.) (Diptera: Tachinidae), a larval parasitoid of Lepidoptera, can be reared from egg to fecund adult on artificial media composed of crude components. The standard in vitro culture is performed in 24‐well plastic rearing plates. Exorista larvarum eggs, removed from superparasitized larvae of Galleria mellonella (L.) (Lepidoptera: Pyralidae), are individually placed in the wells, each containing a cotton swab soaked in liquid medium. The plates are then sealed until parasitoid puparium formation. To avoid contamination by microorganisms, the artificial medium is routinely supplemented with 0.01% solution of gentamicin. Experiments were carried out to assess whether this broad‐spectrum antibiotic may be replaced with hydrolate of Monarda fistulosa L. (Lamiaceae), which was selected due to its high in vitro activity against pathogenic microorganisms for humans and plants. The hydrolate was either supplemented to the artificial medium (0.5% wt/wt) (first experiment) or placed in an empty well (200 μl) of the rearing plate, to be supplied as saturated air due to evaporation (second experiment). In both experiments, a standard medium with gentamicin and an antimicrobial‐free medium were maintained as positive and negative controls, respectively. In the first experiment, in the hydrolate‐supplemented medium fewer E. larvarum completed egg‐to‐adult development than in the standard medium, but significantly more parasitoids developed from egg to adult compared to the antimicrobial‐free medium. No significant difference was found between the numbers of eggs laid by the females obtained from the standard medium vs. those from the hydrolate‐supplemented medium. In the second experiment, the hydrolate‐saturated air significantly decreased E. larvarum egg hatching, puparium formation, and female fecundity compared to the standard medium. In perspective, M. fistulosa hydrolate supplemented to the artificial media for E. larvarum may be considered as a promising candidate to replace the gentamicin solution, as suggested also by the microbiological analyses of the media, performed at various growth stages of the parasitoid in a separate trial. Conversely, the hydrolate‐saturated air treatment was deemed unsuitable.     

Isolation of eukaryotic ribosomal proteins. Purification and characterization of the 60 S ribosomal subunit proteins L4, L5, L7, L9, L11, L12, L13, L21, L22, L23, L26, L27, L30, L33, L35', L37, and L39.

The proteins of the large subunit of rat liver ribosomes were separated into seven groups by stepwise elution from carboxymethylcellulose with LiCl at pH 6.5. Seventeen proteins (L4, L5, L7, L9, L11, L12, L13, L21, L22, L23, L26, L27, L30, L33, L35', L37, and L39) were isolated from three of the groups (B60, D60, G60) by ion exchange chromatography on carboxymethylcellulose and by filtration through Sephadex. The amount of protein obtained varied from 0.5 to 15 mg. Eight of the proteins (L9, L11, L13, L21, L22, L35', L37 and L39) had no detectable contamination; the impurities in the others were no greater than 9%. The molecular weight of the proteins was estimated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate; the amino acid composition was determined.     

Inter-simple sequence repeat (ISSR) diversity within Monarda fistulosa var. brevis (Lamiaceae) and divergence between var. brevis and var. fistulosa in West Virginia

Inter-simple sequence repeat (ISSR) banding patterns were used to examine genetic diversity within and among populations ofMonarda fistulosa var.brevis, a rare taxon restricted to several populations in limestone glades and barrens in eastern West Virginia and Virginia. More than 34% of the total ISSR diversity in var.brevis occurred among populations, which is high when compared to the few other rare species that have been examined for ISSR variation. Prior studies demonstrated that var.brevis is morphologically distinct from the more widespread var.fistulosa, and that the differences are maintained when the two varieties are grown together in a uniform environment. The present study utilizing ISSR markers indicated that the two varieties are distinct, though quite similar genetically, and this is concordant with prior investigations documenting their morphological and habitat differences. However, the ISSR results suggest that the two varieties have diverged relatively recently and/or there is a low level of gene flow between them.     

The complete primary structure of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus

The amino acid sequences of ribosomal proteins L1, L14, L15, L23, L24 and L29 from Bacillus stearothermophilus have been completely determined. This has been achieved by sequence analyses of peptides derived from enzymatic digestions of the proteins with trypsin, chymotrypsin, pepsin, Staphylococcus aureus protease, and Armillaria mellea protease as well as by chemical cleavage with hydroxylamine and cyanogen bromide. Based on the primary structures of the six proteins, their secondary structures were predicted using four different computer prediction programs. A comparison of the amino acid sequences of the studied proteins from B. stearothermophilus with the homologous proteins from Escherichia coli revealed that in four proteins (L1, L15, L24 and L29) between 40-50% of the residue in the sequences are identical, whereas this value is significantly higher (69%) for L14 and lower (28%) for L23. The distribution of those amino acid residues which are identical in the corresponding proteins from the two bacteria is not random along the protein chain: some regions are highly conserved whereas others are not. This finding indicates that the regions which are conserved during evolution are important for the spatial structure and/or function of the protein.     

Sequence of the amino-terminal region of rat liver ribosomal proteins S4, S6, S8, L6, L7a,L18, L27, L30, L37, L37a,and L39

The sequence of the amino-terminal region of eleven rat liver ribosomal proteins–S4, S6, S8, L7a, L18, L27, L30, L37a, and L39 - was determined. The analysis confirmed the homogeneity of the proteins and suggests that they are unique, since no extensive common sequences were found. The N-terminal regions of the rat liver proteins were compared with amino acid sequences in Saccharomyces cerevisiae and in Escherichia coli ribosomal proteins. It seems likely that the proteins L37 from rat liver and Y55 from yeast ribosomes are homologous. It is possible that rat liver L7a or L37a or both are related to S cerevisiae Y44, although the similar sequences are at the amino-terminus of the rat liver proteins and in an internal region of Y44. A number of similarities in the sequences of rat liver and E coli ribosomal proteins have been found; however, it is not yet possible to say whether they connote a common ancestry.     

Localization of proteins L4, L5, L20 and L25 on the ribosomal surface by immuno-electron microscopy

Summary Ribosomal proteins L4, L5, L20 and L25 have been localized on the surface of the 50S ribosomal subunit of Escherichia coli by immuno-electron microscopy. The two 5S RNA binding proteins L5 and L25 were both located at the central protuberance extending towards its base, at the interface side of the 50S particle. L5 was localized on the side of the central protuberance that faces the L1 protuberance, whereas L25 was localized on the side that faces the L7/L12 stalk. Proteins L4 and L20 were both located at the back of the 50S subunit; L4 was located in the vicinity of proteins L23 and L29, and protein L20 was localized between proteins L17 and L10 and is thus located below the origin of the L7/L12 stalk.     

Structural comparison of the prokaryotic ribosomal proteins L7/L12 and L30

The structures of two prokaryotic ribosomal proteins, the carboxyterminal half of L7/L12 from Escherichia coli (L12CTF) and L30 from Bacilus stearothermophilus display a remarkably similar fold in which alpha-helices pack onto one side of an antiparallel, three-stranded, beta-pleated sheet. A detailed comparison of the structures by least-squares methods reveals that more than two-thirds of the alpha carbons can be superimposed with a root mean square distance of 2.33 A. The principal difference is an extra alpha-helix in L12CTF. The sequences of the proteins display a distinct conservation in regions which are crucial to the common fold, in particular the hydrophobic core. It is proposed that the similarity is a result of divergent evolution.     

Direct Organogenesis and Plant Regeneration in Preconditioned Tissue Cultures of Lathyrus cicera L., L. ochrus (L.)DC. and L. sativus L.

This study demonstrates the importance of preconditioning ofsource tissue in regeneration of multiple shoot buds from severalspecies of Lathyrus. Preconditioned multiple shoots of Lathyruscicera L., L. ochrus (L.) DC. and L. sativus L. were obtainedby germinating seeds on Murashige and Skoog (MS) medium containing50 µM N⁵-benzylaminopurine (BAP) for 2 to 3 weeks. Multipleshoot bud formation occurred when epicotyl explants of preconditionedshoots were cultured on MS medium containing 5–50 µMBAP. No shoot regeneration was observed from epicotyl explantswhich were obtained from non-preconditioned shoots. Shoot budswere formed directly on explants without an intervening callusphase after 2 to 3 weeks of culture. Regenerated shoot budsformed healthy shoots which developed prolific and strong rootswhen transferred to MS medium supplemented with 2.5 µMnaphthaleneacetic acid (NAA). Lathyrus cicera L., L. ochrus (L.) DC., Ochrus Vetch, L. sativus L., Lathyrus pea, de novo differentiation, epicotyl, preconditioning with BAP     

Structural alteration of rRNA in the L7/L12 region of 50s ribosome on removal of L7/L12 proteins

Core particles of 50S ribosomes depleted of $\text{L7}\text{L12}$ proteins are degraded by RNase I at a considerably slower rate than intact 50S ribosomes. The normal rate is restored on incorporating $\text{L7}\text{L12}$ proteins into the core particles. The capacity of the core particles to inhibit the RNase I-catalyzed hydrolysis of poly A and to bind ethidium bromide is also greater with core particles than with intact 50S ribosomes. It appears from these results that the region(s) of rRNA in the vicinity of $\text{L7}\text{L12}$ proteins has less ordered structure which, on removal of $\text{L7}\text{L12}$ proteins, becomes more organized. Apparently, binding of $\text{L7}\text{L12}$ proteins to the 50S core leads to the destabilization of double-stranded regions of rRNA.     

Molecular phylogenies based on ribosomal protein L11, L1, L10, and L12 sequences

Summary Available sequences that correspond to the E. coli ribosomal proteins L11, L1, L10, and L12 from eubacteria, archaebacteria, and eukaryotes have been aligned. The alignments were analyzed qualitatively for shared structural features and for conservation of deletions or insertions. The alignments were further subjected to quantitative phylogenetic analysis, and the amino acid identity between selected pairs of sequences was calculated. In general, eubacteria, archaebacteria, and eukaryotes each form coherent and well-resolved nonoverlapping phylogenetic domains. The degree of diversity of the four proteins between the three groups is not uniform. For L11, the eubacterial and archaebacterial proteins are very similar whereas the eukaryotic L11 is clearly less similar. In contrast, in the case of the L12 proteins and to a lesser extent the L10 proteins, the archaebacterial and eukaryotic proteins are similar whereas the eubacterial proteins are different. The eukaryotic L1 equivalent protein has yet to be identified. If the root of the universal tree is near or within the eubacterial domain, our ribosomal protein-based phylogenies indicate that archaebacteria are monophyletic. The eukaryotic lineage appears to originate either near or within the archaebacterial domain. Correspondence to: P. Dennis