Immunocytochemical localisation of vitellogenic and non-vitellogenic yolk proteins in the ovary of leptinotarsa decemlineata

• 1.1. Two vitellogenins and chromoprotein 2 are selectively accumulated by the oocyte and cannot be detected either in follicle cells or in the germarium.
• 2.2. At the start of their accumulation in terminal oocytes they are asymmetrically distributed.
• 3.3. Endocytosis of vitellogenin 1 starts somewhat later than the uptake of vitellogenin 2 and chromoprotein 2.
• 4.4. In follicle cells of young follicles, a protein (DLP), immunologically related to diapause protein 1, is highly concentrated.
• 5.5. During vitellogenesis DLP is sequestered by the oocytes.
• 6.6. The protein rich globules in terminal oocytes contain the vitellins as well as chromoprotein 2 and DLP.

     

Solvent perturbation spectra of yellow mealworm α-amylase and of wheat protein inhibitors

• 1.1. The number of tyrosine and tryptophan residue-equivalents on the surfaces of the α-amylase and of two of its protein inhibitors has been determined.
• 2.2. The solvent-exposed tyrosine and tryptophan residue-equivalents in the dimeric inhibitor are respectively four and two times as much as those ones of the monomeric inhibitor.
• 3.3. On the basis of the homology among their polypeptide chains, it is suggested that the outer tryptophan residues in either inhibitors are located at the positions 4 and 51 of the primary structure.
• 4.4. On the interaction of the monomeric inhibitor with the amylase, two tryptophan residue-equivalents became no more accessible to the solvent.

     

Domain structure of the 90-kDa stress protein: Heparin- and antibody-binding domain

• 1.1. To understand the physiological roles of the 90-kDa stress protein (HSP90), we investigated the heparin- and antibody-binding domains of the protein.
• 2.2. For heparin-binding sites, HSP90 was digested completely with trypsin, and the digests were applied to a heparin-Sepharose column and eluted with 1.0 M NaCl, followed by 8.0 M urea.
• 3.3. Each elutant was purified by a reverse-phase C₁₈ column.
• 4.4. Two peptides from the NaCl-eluted fraction and no peptide from the urea-eluted fraction were purified.
• 5.5. The purified peptides were sequenced by an automated peptide sequencer.
• 6.6. One of the heparin-binding sites was present between Leu-362 and Arg-365; another was present between Leu-645 and Lys-648.
• 7.7. These two peptides were basic and considerably hydrophilic.
• 8.8. For antibody-binding sites, HSP90 was mildly digested with trypsin, electrophoresed on SDS-polyacrylamide gels and transferred to PVDF membranes.
• 9.9. The four bound of the trypsin fragments could be sequenced with a peptide sequencer.
• 10.10. There was only one antibody-binding peptide, 38 kDa, starting from Pro-2. The others showed no cross-reactivity with the antibody and started from Leu-283.
• 11.11. Therefore, the epitopes of HSP90 are present between Pro-2 and Leu-282.
• 12.12. The heparin-binding sites are present from the middle region of the HSP90 molecule, and the antigen sites are at the N-terminal domain.

     

Expression of a P0-like glycoprotein in central nervous system myelin of amphibians (Ambystoma mexicanus,xenopus laevis and Rana catesbeiana)

• 1.1. The myelin protein profiles in the CNS and PNS of three species of amphibians were analyzed by biochemical and immunohistochemical methods.
• 2.2. The CNS myelin of the African clawed frog (Xenopus) and the Mexican salamander (axolotl) contained, in addition to proteolipid protein, a unique protein zero (P0)-like protein, whereas the adult bullfrog did not.
• 3.3. A strong expression of the P0-like protein in the bullfrog CNS myelin was found transiently at ontogenetically early phases including at the time of metamorphosis.
• 4.4. The CNS P0-like protein and the PNS P0 protein showed a difference in reactivity with lectins and anti-L2/HNK-1 antibodies, suggesting that the two proteins differ in some aspects of their carbohydrate structures.

     

Crystalline style proteins from bivalve molluscs

• 1.1. Proteins from crystalline styles of twelve species of bivalve mollusc were examined under different gel electrophoresis conditions and stained to reveal both protein and carbohydrate.
• 2.2. Native extracts of styles produced relatively few protein bands, however denaturation with SDS resulted in much more complex zymograms.
• 3.3. All species possessed several prominent high mol wt glycoproteins.
• 4.4. Eulamellibranchia all had a major non-glycosylated protein at approx. 62,000 mol. wt.
• 5.5. Most Filibranchia had a major non-glycosylated protein at 37,000–50,000 mol. wt.
• 6.6. Eulamellibranchia were a much more homogeneous group than the Filibranchia.

     

Effect of lindane on phosphatidylinositol synthesis by cerebral cortex after acute and subchronic treatment

• 1.1. The incorporation of myo-[2-³H]inositol into phosphatidylinositols was unmodified in brain cortex miniprisms from convulsant rats.
• 2.2. However, the incorporation had increased by 300–400% in non convulsant rats which had received the same amount of lindane at a lower concentration.
• 3.3. This result suggests that phosphatidylinositols are implicated in the convulsion syndrome.
• 4.4. Experiments with lindane added in vitro were performed with both subchronically lindane intoxicated and untreated rats.
• 5.5. The results show an interesting lack of parallelism.
• 6.6. This might indicate the development of some resistance to the effects of lindane, possibly as the result of complex compensatory changes in inositol lipid biosynthesis.

     

Identification and characterization of vitellin in a hermophrodite shrimp,Pandalus kessleri

• 1.1. A female specific protein (FSP, vitellogenin) in hemolymph and its related ovarian protein (vitellin) of Pandalus kessleri were studied by means of electrophoretical and immunological procedures.
• 2.2. The vitellin was purified from vitellogenic ovaries using hydroxylapatite, DEAE cellulose and Sepharose 6B columns, consecutively.
• 3.3. The vitellin had a molecular weight of approximately 560 kD and was composed of two subunits, 81 and 110 kD, respectively.
• 4.4. The vitellogenin concentrations in the hemolymph increased as vitellogenesis in the ovarian oocytes advanced and dropped markedly after the release of mature eggs.

     

Physicochemical property of bovine brain 73-kDa stress protein

• 1.1. An approximately 70-kDa protein was purified from bovine brain using an ATP-Sepharose column.
• 2.2. The protein sample was found to contain two proteins (major 73 kDa and minor 72 kDa) on two-dimensional gel electrophoresis.
• 3.3. Antibodies raised against the 73- and 72-kDa proteins cross-reacted with stress-induced HSP73 and HSP72 from HeLa cells, respectively.
• 4.4. Heparin-binding peptides were obtained from trypsin digests of HSP73.

     

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Phosphorylation of Escherichia coli proteins during the SOS response

• 1.1. The phosphorylation of Escherichia coli proteins was analyzed comparatively before and after induction of the SOS response in a temperature-sensitive mutant strain.
• 2.2. The presence of phosphorylated proteins was evidenced by gel electrophoresis and autoradiography after labelling with radioactive orthophosphate in vivo or radioactive adenosine triphosphate in vitro.
• 3.3. Significant changes in the intensity of protein labelling were observed upon induction of the SOS functions: six proteins were found to be more phosphorylated while two others were less phosphorylated. Moreover, five additional proteins appeared to become phosphorylated exclusively during the SOS response. The molecular mass and isoelectric point of these various proteins were determined.
• 4.4. For most proteins, the changes in the pattern of protein phosphorylation were concomitant with variations in the amount of protein synthesized.
• 5.5. The changes in the pattern of phosphoproteins observed during the SOS response were not due to the temperature shift required experimentally for expressing the SOS phenotype.
• 6.6. Phosphorylation was found to be catalyzed by protein kinases that modify amino acid residues at hydroxyl groups in protein substrates.
• 7.7. Both in vivo and in vitro studies brought evidence that neither RecA nor LexA, the two key regulatory proteins of the SOS functions, were capable of undergoing phosphorylation.

     

Properties of the transition from short-term to long-term depression in neurons of Helix pomatia

• 1.1. Synaptic short-term depression could be transferred into long term depression by repetition of series of stimuli.
• 2.2. The transition from short-term depression to long-term depression was blocked by puromycin.
• 3.3. The majority of the transition took place during resting periods between stimulus series.
• 4.4. The initiation of the transition process was 83% completed after 5 min of stimulation.
• 5.5. Short- and long-term depression were quantitatively separated into their two serial sites of origin: afferent axons and synaptic terminals.
• 6.6. Long sequences evoked periods with increased and variable EPSPs not conforming to depression.

     

Identification of the major annexins in Ehrlich ascites tumor cells

• 1.1. Three calcium-binding proteins have been purified from Ehrlich ascites tumor cells.
• 2.2. They were identified by amino acid sequence analysis on selected fragments obtained by tryptic digestion.
• 3.3. The proteins belong to the annexin family and were identified as annexins II, III and V.
• 4.4. Antibodies raised against the proteins were used to examine for their presence in a number of murine tissues.
• 5.5. The occurrence was found to be in reasonable accordance with earlier reports.

     

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Main serum protein of rainbow trout (Salmo gairdnerii): its biological properties and significance

• 1.1. Main serum α₁-protein (α₁P) of rainbow trout was purified and its biochemical and physico-pathological properties were studied.
• 2.2. α₁P was suggested to be a primitive protein having both properties of albumin and AFP in serum proteins of mammals according to the following results.
• 3.3. Molecular weight (75,000), two kinds of molecules (pI 4.55 and 5.05) and amino acid composition.
• 4.4. Dye- or ConA binding activity.
• 5.5. Estrogen binding activity and inhibitory effect on lymphoblastoid-forming activity.
• 6.6. Possible osmotic regulator.
• 7.7. Significant elevation of blood α₁P level in the course of hepatoma induction.

     

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Purification and characterization of vitellogenin from the American cockroach,Periplaneta americana

• 1.1. Vitellogenin (VG) was isolated and purified from the hemolymph of female American cockroaches.
• 2.2. The purification method used in this study comprises two steps: the first step is based on the method originally developed for purifying lipophorin from hemolymph, and the second step is the separation of VG from lipophorin by a KBr density gradient ultracentrifugation.
• 3.3. The purified VG was characterized according to molecular weight, substructure, shape and size, and lipid composition.
• 4.4. The VG molecule is almost globular in shape with the diameter of about 15.5 nm and is indistinguishable from lipophorin in shape and size.
• 5.5. The native molecular weight determined by light scattering method was 560 kDa.
• 6.6. The VG consists of four subunits with molecular weights of approximately 102, 81, 49 and 40 kDa, respectively.
• 7.7. VG is a lipoprotein and comprises 92% protein and 8% lipid.
• 8.8. Major lipid components were found to be diacylglycerol (25%) and phospholipids (71%).

     

δ-Aminolevulinic acid dehydratase inactivation by uroporphyrin I in light and darkness

• 1.1. The action of uroporphyrin I on erythrocytic ALA-D activity under dark and light conditions was examined.
• 2.2. Photo and non-photoinactivation of ALA-D induced by uroporphyrin I were observed.
• 3.3. Both effects were dependent on uroporphyrin concentration, temperature and time of exposure of the protein to the porphyrin.
• 4.4. Light-dependent effect of uroporphyrin I is related with the phototoxicity of porphyrins and could be produced by primary amino acid photooxidation followed by secondary cross-linking of the protein.
• 5.5. Light-dependent effect of uroporphyrin I could be ascribed to a direct enzyme inhibition due to binding of the porphyrin to the protein inducing structural changes at or near its active site.