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: 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

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:20) 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: Agent for the detection of esterolytic and/or proteolytic enzymes, containing (a) an amino acid ester or peptide ester of a phenol, as the chromogenic enzyme substrate, and (b) an alcohol as the substance which accelerates the enzymatic cleavage of the amino acid ester bond or peptide ester bond of component (a), characterized in that it contains a salt as the accelerating substance.

Abstract: A new method of determining oxidized .alpha.-1-proteinase inhibitor in serum or plasma for use in studying the development of chronic obstructive lung disease is disclosed. Levels of oxidized .alpha.-1-proteinase inhibitor indicate the potential for emphysema development with higher levels showing a decrease in lung protection against elastolytic enzymes such as elastase. This method can be used for patients with a potential for chronic obstructive lung disease rather than having to use bronchial lavage methods for such patients. No other method is known to exist for determining oxidized .alpha.-1-proteinase inhibitor in serum or plasma.

Abstract: A new method of determining oxidized .alpha.-1-proteinase inhibitor in serum or plasma for use in studying the development of chronic obstructive lung disease is disclosed. Levels of oxidized .alpha.-1-proteinase inhibitor indicate the potential for emphysema development with higher levels showing a decrease in lung protection against elastolytic enzymes such as elastase. This method can be used for patients with a potential for chronic obstructive lung disease rather than having to use bronchial lavage methods for such patients. No other method is known to exist for determining oxidized .alpha.-1-proteinase inhibitor in serum or plasma.

Abstract: Certain compositions have been prepared by the reaction of certain dyes of the class generally known as Color Index reactive dyes with certain support phases. The dyes utilized for said compositions all possess the general sulfanilido-triazidinyl-sulfoaryl group wherein the aryl groups may be phenyl or naphthyl and said general group is further bonded to aryl groups via an amino or azo linkage. It has been found that when aqueous fluids containing albumin, such as, for example, plasma or serum are passed over compositions within the scope of the present invention albumin is selectively adsorbed on said compositions without removal of other proteins present in the fluid. It has further been found that the albumin may be readily removed from the thus formed adsorbate without denaturing the albumin and leaving the solid phase dye composition in a suitable state for re-use without loss of activity.

Abstract: Certain compositions have been prepared by the reaction of certain dyes of the class generally known as Color Index reactive dyes with certain support phases. The dyes utilized for said compositions all possess the general sulfanilido-triazidinyl-sulfoaryl group wherein the aryl groups may be phenyl or naphthyl and said general group is further bonded to aryl groups via an amino or azo linkage. It has been found that when aqueous fluids containing albumin, such as, for example, plasma or serum are passed over compositions within the scope of the present invention albumin is selectively adsorbed on said compositions without removal of other proteins present in the fluid. It has further been found that the albumin may be readily removed from the thus formed adsorbate without denaturing the albumin and leaving the solid phase dye composition in a suitable state for re-use without loss of activity.