Identification,characterization, and developmental profile of a high molecular weight,juvenile hormone-binding protein in the hemolymph of the migratory grasshopper,Melanoplus sanguinipes

In the hemolymph of Melanoplus sanguinipes, a high molecular weight juvenile hormone binding protein (JHBP) was identified by photoaffinity labelling and found to have a M_r of 480,000. The JHBP, purified using native gel electrophoresis followed by electroelution, has an equilibrium dissociation constant for JH III of 2.1 nM and preferentially binds JH III over JH I. Antibody raised against JHBP recognized only the 480,000 band. Under denaturing conditions the native JHBP gave a single band with a M_r 78,000. The antibody against native JHBP recognized only the 78,000 protein in SDS-treated hemolymph samples, indicating that JHBP is a hexamer in this species. The concentration of JHBP fluctuates in both the sexes during nymphal and adult development in parallel with total protein content of hemolymph. © 1995 Wiley-Liss, Inc.     

Cell surface T antigen in cells infected with simian virus 40 or an adenovirus-simian virus 40 hybrid, Ad2+D2.

Cell surface T antigen, detected by a radioimmune assay that uses 125I-labeled Staphylococcus aureus protein A and antibodies against either authentic T antigen or D2 hybrid T antigen, was found in simian virus 40-transformed and -infected cells and in cells infected with an adenovirus-simian virus 40 hybrid, Ad2+D2. In simian virus 40 lytic infection, the surface T antigen appeared at the same time as the nuclear T antigen.     

Physiology and characterization of a fungal milk-clotting enzyme from Aspergillus flavus.

Aspergillus flavus produced extracellularly an active rennin-like enzyme when grown aerobically in whey media. The enzyme was detected at early stages of growth reaching a maximum after three to four days at 25 degrees. The activity was destroyed by heating to temperatures higher than 50 degrees, whereas the presence of skim milk during heating preserved the enzyme activity, at least, up to 70 degrees. Calcium chloride significantly stimulated the milk-clotting activity up to 1% final concentration. The clotting time was inversely proportional to protein concentration in the range 0.2-0.6 mg/ml and the enzyme exhibited marked stability when stored at 37 degrees at pH 6.     

Kinetic studies on the diaqua form of cis-platin and various nucleobases

Kinetic studies on cis-[Pt(NH3)2(OH2)2]2+ and various nucleobases show that this ion reacts more quickly with guanosine than with adenosine, cytidine, and thymidine, and that a monophosphoric acid unit considerably enhances the rate of reaction of guanosine; the kinetic preference of 5'-GMP over 5'-AMP may point to a greater thermodynamic selectivity.     

Cytological lesions in the midgut of Tribolium confusum larvae exposed to gamma radiation

The major cytological lesions in Tribolium confusum after irradiation were displayed by the midgut epithelium. At 24 hr following exposure to 5.3 kR, the regenerative cells called nidi appeared numerous. They gradually disappeared with increases in dosage and time in accordance with Arndt-Schulze's Law. The columnar epithelial cells and their nuclei appeared swollen and vacuolated on the fifth and twelfth day following exposure to 5.3 kR. They appeared disorganized and shed into the lumen of the midgut on the twelfth and fifth day following 50- and 70-kR irradiation, respectively. The basement membrane and the muscularis appeared loose on the fifth and twelfth day following 70-kR irradiation. It was observed that once the catabolic activity, i.e., histolysis, was initiated in the midgut, it continued to accelerate with increasing dose and time. Thus, the late effects at low doses, 5.3 and 10 kR, appeared as immediate effects at high doses, 50 and 70 kR. The differentiated cells, i.e., columnar epithelial cells, appeared radioresistant as compared to undifferentiated cells, i.e., regenerative cells, which appeared radiosensitive in accordance with the principle of Bergonie and Tribondeau.     

Effect of design dark fraction on the loss of biomass productivities in photobioreactors

Bioprocess and Biosystems Engineering - Design dark fraction reflects the unlit part of a microalgal culture system, as for example a hydraulic loop used for temperature or pH regulation, or a...     

Inositol‐requiring enzyme‐1 regulates phosphoinositide signaling lipids and macrophage growth

The ER‐bound kinase/endoribonuclease (RNase), inositol‐requiring enzyme‐1 (IRE1), regulates the phylogenetically most conserved arm of the unfolded protein response (UPR). However, the complex biology and pathology regulated by mammalian IRE1 cannot be fully explained by IRE1’s one known, specific RNA target, X box‐binding protein‐1 (XBP1) or the RNA substrates of IRE1‐dependent RNA degradation (RIDD) activity. Investigating other specific substrates of IRE1 kinase and RNase activities may illuminate how it performs these diverse functions in mammalian cells. We report that macrophage IRE1 plays an unprecedented role in regulating phosphatidylinositide‐derived signaling lipid metabolites and has profound impact on the downstream signaling mediated by the mammalian target of rapamycin (mTOR). This cross‐talk between UPR and mTOR pathways occurs through the unconventional maturation of microRNA (miR) 2137 by IRE1’s RNase activity. Furthermore, phosphatidylinositol (3,4,5) phosphate (PI(3,4,5)P₃) 5‐phosphatase‐2 (INPPL1) is a direct target of miR‐2137, which controls PI(3,4,5)P₃ levels in macrophages. The modulation of cellular PI(3,4,5)P₃/PIP₂ ratio and anabolic mTOR signaling by the IRE1‐induced miR‐2137 demonstrates how the ER can provide a critical input into cell growth decisions.     

Recognition of gluconeogenic enzymes; Icl1, Fbp1, and Mdh2 by Gid4 ligase: A molecular docking study

The pro/N‐degron pathway is an evolved protein degradation pathway through the ubiquitin‐proteasome system. It is a vital pathway to attain protein homeostasis inside the liver cells with varying glucose levels. N‐terminal proline exists in more than 300 proteins in Saccharomyces cerevisiae, but only three of them are the gluconeogenic enzymes; isocitrate lyase (Icl1), fructose‐1,6‐bisphosphatase (Fbp1), and malate dehydrogenase (Mdh2). The present in silico study aims to structurally illustrate the binding of Icl1 enzyme to Gid4 ligase concerning its peers; Fbp1 and Mdh2. Based on the molecular docking scores and interactions, one can attribute the binding stability of Gid4 with degrons, to peptides of length six up to eight from the N‐terminal. Moreover, the percent change in the docking score provides a rationale for the unique Gid4‐Icl1^1‐4 interaction. The present study provides insights on the binding attitude of Gid4 ligase to degrons of different lengths, so one will consider in designing peptidomimetics to target Gid4 ligase.