Abstract: The invention provides a fiber blend, spun yarn, and textile material comprising a plurality of cellulosic fibers and a plurality of first synthetic fibers. The first synthetic fibers comprise a polyoxadiazole polymer, and the polyoxadiazole polymer comprises a plurality of first repeating units and a plurality of second repeating units, the first repeating units conforming to the structure of Formula (I) below and the second repeating units conforming to the structure of Formula (II) below Y is selected from the group consisting of chlorine, bromine, diphenylphosphine oxide, and diphenylphosphine sulfide. The invention also provides a method for protecting an individual from infrared radiation that can be generated during an electrical arc flash using such a textile material.

Abstract: A flame resistant textile is provided. The textile is a sateen weave fabric containing cellulosic fibers, where the sateen weave fabric has a thickness of at least 19.5 mils, a thickness of at least 25 mils after 3 home washes at 120° F., an air permeability of at least 60 cfm, and a weight of less than about 7 oz/yd2. The sateen weave fabric also contains a treatment, where the treatment contains a tetramethylhydroxy phosphonium salt or its condensate and chemical selected from the group consisting of urea, guanidines, guanyl urea, glycoluril, and polyamines. When the sateen weave fabric to which the treatment has been applied has been heat-cured and oxidized at least a portion of the cellulosic fibers have a pentavalent phosphate compound polymerized therein. The method for producing the flame resistant textile is also provided.

Abstract: A load carrier with a retracting elongate securement device, the load carrier having a support arrangement with a vehicle interfacing portion and a load support interfacing portion, as well as a load support which interfaces with the support arrangement. The load support is configured to receive and carry cargo loads thereupon and has an elongate tubular member having an extendible member received therein. The load carrier further has a biasing member operatively interposed between the elongate tubular member and the extendible member, the biasing member exerting a retracting force on the extendible member thereby urging the extendible member to a retracted configuration within the elongate tubular member.

Abstract: Flame resistant fabrics of suitable strength and comfort level for use in apparel applications. The fabrics incorporate yarns utilizing specific blends of (A) halogen containing fibers, (B) silica embedded cellulosic fibers and (C) strength imparting synthetic fibers.

Abstract: Flame resistant fabrics of suitable strength and comfort level for use in apparel applications. The fabrics incorporate yarns utilizing specific blends of (A) halogen containing fibers, (B) silica embedded cellulosic fibers and (C) strength imparting synthetic fibers.

Abstract: Synchronous digital ink and audio annotations of media data stream. A media data stream is rendered. The media data stream includes media data organized in one or more segments. Annotating data is received from a user for annotating the media data. A time is identified when the annotating data is received. The identified time is relative to a time corresponding to the one or more segments of the media data as the media data stream is being rendered. An annotating data stream is organized to include the annotating data synchronized with the media data stream based on the identified time. A new file is created that includes the original media data stream and the annotating data stream, or the annotating data stream is added to the original file and saved to a storage area.

Abstract: The present invention provides isolated polypeptides, prolyl tripeptidyl-peptidases, and active analogs, active fragments or active modifications thereof, having amidolytic activity for cleavage of a peptide bond present in a target peptide having at least 30 amino acids. Isolated nucleic acid fragments encoding isolated prolyl tripeptidyl-peptidases are also provided, as are methods of reducing growth of a bacterium by inhibiting a prolyl tripeptidyl-peptidase.

Abstract: The present invention provides isolated polypeptides, dipeptidylpeptidases, active analogs, active fragments, or active modifications thereof, having amidolytic activity for cleavage of a peptide bond between the second and third amino acids from the N-terminal end of a target polypeptide, wherein the target polypeptide has an aliphatic or an aromatic residue as a substituent on the ?-carbon atom of the second amino acid from the N-terminal end of the peptide. Isolated nucleic acids encoding dipeptidylpeptidases are also provided, as are methods of reducing growth of a bacterium by inhibiting a dipeptidylpeptidase.

Abstract: An isolated oral bacterial polypeptide having amidolytic activity for cleavage of denatured polypeptides and nondenatured serpin polypeptides and particularly a human &agr;1-proteinase inhibitor polypeptide is provided. The mature polypeptide of the invention has a molecular weight of about 70 kD to about 80 kD. Also provided is an isolated nucleic acid sequence encoding the oral bacterial polypeptide of the invention, methods for identifying inhibitors of the polypeptide and compositions such as immunogenic compositions and inhibitor compositions.

Abstract: Methods for controlling blood coagulation, and suitable pharmaceutical compositions that include a polypeptide that enhances the anticoagulation process (or inhibitors thereof for reversing the anticoagulation process) are provided.

Abstract: The present invention provides isolated polypeptides, dipeptidylpeptidases, active analogs, active fragments, or active modifications thereof, having amidolytic activity for cleavage of a peptide bond between the second and third amino acids from the N-terminal end of a target polypeptide, wherein the target polypeptide has an aliphatic or an aromatic residue as a substituent on the &agr;-carbon atom of the second amino acid from the N-terminal end of the peptide. Isolated nucleic acids encoding dipeptidylpeptidases are also provided, as are methods of reducing growth of a bacterium by inhibiting a dipeptidylpeptidase.

Abstract: The present invention provides polypeptides, including chymotrypsin-like polypeptides and elastase-like polypeptides, having amidolytic acitivity for cleavage of a peptide bond present in a target polypeptide. The polypeptides can be isolated from ants, including S. invicta larvae. Isolated nucleic acid fragments encoding isolated polypeptides are also provided, as are methods of developing and using inhibitors of chymotrypsin-like polypeptides and elastase-like polypeptides.

Abstract: Provided herein is a nucleotide sequence encoding an Arg-specific gingipain, said Arg-gingipain characterized as having an apparent molecular mass of 50 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and an apparent molecular mass of 44 kDa as estimated by gel filtration chromatography, said gingipain-1 having amidolytic and proteolytic activity for cleavage after arginine residues and having no amidolytic and/or proteolytic activity for cleavage after lysine residues, wherein the amidolytic and/or proteolytic activity is inhibited by cysteine protease group-specific inhibitors including iodoacetamide, iodoacetic acid, N-ethylmaleimide, leupeptin, antipain, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, TLCK, TPCK, p-aminobenzamidine, N-chlorosuccinamide, and chelating agents including EDTA and EGTA, wherein the amidolytic and/or proteolytic activity of said gingipain-1 is not sensitive to inhibition by human cystatin C, &agr;2-macroglobulin, &agr;1-proteinase inhibitor,

Abstract: Provided herein are methods and immunogenic compositions useful for protecting mammals from infection and pathology of P. gingivalis. Specifically, arginine-specific proteases of Porphyromonas gingivalis and peptides derived therefrom offer protection against infection. Immunogenic compositions comprising a 50 kDa arginine-specific protease, the high molecular weight complex or peptides from one of the foregoing proteins are capable of protecting against P. gingivalis infection and/or gingivitis and/or periodontitis caused thereby in mammals, including humans.

Abstract: Provided herein is a Porphyromonas gingivalis high molecular weight arginine-specific proteinase comprising a protease component of 50 kD and a hemagglutinin component of about 44 kD as estimated by SDS-PAGE. The proteinase is stimulated by glycine containing peptides and glycine analogues. It is inhibited by cysteine protease group specific inhibitors.

Abstract: A process and apparatus for separating tritium from an aqueous solution that contains one or more additional dissolved radionuclides is disclosed. In accordance with the process the aqueous solution as a first liquid phase is contacted with each of three layers as a solid phase within a column. A first layer comprises particles having a plurality of pendent methylene diphosphonate groups. A second layer comprises strongly basic anion exchange particles, and a third layer comprises polymer particles free of ionically charged groups. The contact is maintained until a second liquid phase is formed that contains tritium as substantially the only radionuclide, and that second liquid phase is collected and can then be counted to determine the amount of tritium present. The column with its three layers constitutes the separation apparatus.

Abstract: Peptides which exhibit antimicrobial activity comparable to certain known antibiotics are provided. These peptides are related in sequence to amino acid sequences within Cathepsin G. A broad spectrum bactericidal peptide disclosed herein is RPGTLCTVAGWGRVSMRRGT (SEQ ID NO:22). It is active against Pseudomonas aeruginosa, Neisseria gonorrhoeae and Staphylococcus aureus. RRENTQQHITARRAIRHPQY (SEQ ID NO:19) and GKSSGVPPEVFTRFVSSFLPWIRTTMR (SEQ ID NO:26) also exhibited potent activity against P. aeruginosa strains, including clinical isolates. IIGGR (SEQ ID NO:1) and IVGGR (SEQ ID NO:2) act against both gram-negative and gram-positive bacterial strains. HPQYNQR (SEQ ID NO:3) and certain related peptides are also active against both gram-negative and gram-positive bacteria, including, but not limited to, strains of Escherichia coli, Neisseria gonorrhoeae, Staphylococcus aureus, Capnocytophage sputigena and Pseudomonas aeruginosa.

Abstract: Provide herein is a substantially pure Lys-gingipain complex preparation, Lys-gingipain being characterized as having an apparent molecular mass of 105 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, where sample is prepared without boiling, said Lys-gingipain having amidolytic and proteolytic activity for cleavage after lysine residues and having no amidolytic and/or proteolytic activity for cleavage after arginine residues, wherein the amidolytic and/or proteolytic activity is inhibited by TLCK, cysteine protease group-specific inhibitors including iodoacetamide and iodoacetic acid, wherein the amidolytic and/or proteolytic activity of said Lys-gingipain is not sensitive to inhibition by leupeptin, antipain, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, serine protease group-specific inhibitors including diisopropylfluorophosphate and phenylmethyl sulfonylfluoride, and antibodies specific for the Lys-gingipain protein complex and its catalytic component, methods for p

Abstract: Provide herein is a substantially pure gingipain-1 preparation, gingipain-1 being characterized as having an apparent molecular mass of 50 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and an apparent molecular mass of 44 kDa as estimated by gel filtration chromatography, said gingipain-1 having amidolytic and proteolytic activity for cleavage after arginine residues and having no amidolytic and/or proteolytic activity for cleavage after lysine residues, wherein the amidolytic and/or proteolytic activity is inhibited by cysteine protease group-specific inhibitors including iodoacetamide, iodoacetic acid, N-ethylmaleimide, leupeptin, antipain, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, TLCK, TPCK, p-aminobenzamidine, N-chlorosuccinamide, and chelating agents including EDTA and EGTA, wherein the amidolytic and/or proteolytic activity of said gingipain-1 is not sensitive to inhibition by human cystatin C, .alpha.2-macroglobulin, .alpha.

Abstract: Provide herein is a substantially pure Lys-gingipain complex preparation, Lys-gingipain being characterized as having an apparent molecular mass of 105 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, where sample is prepared without boiling, said Lys-gingipain having amidolytic and proteolytic activity for cleavage after lysine residues and having no amidolytic and/or proteolytic activity for cleavage after arginine residues, wherein the amidolytic and/or proteolytic activity is inhibited by TLCK, cysteine protease group-specific inhibitors including iodoacetamide and iodoacetic acid, wherein the amidolytic and/or proteolytic activity of said Lys-gingipain is not sensitive to inhibition by leupeptin, antipain, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, serine protease group-specific inhibitors including diisopropylfluorophosphate and phenylmethyl sulfonylfluoride, and antibodies specific for the Lys-gingipain protein complex and its catalytic component, methods for p