Abstract: The disclosed methods address the identification and monitoring of cancer in a subject using serum peptide profiles. Such profiles allow the detection of the differential presence of certain serum peptide markers in comparison with controls. The profiles can be determined employing mass spectrometry.

Abstract: The disclosed methods address the identification and monitoring of cancer in a subject using serum peptide profiles. Such profiles allow the detection of the differential presence of certain serum peptide markers in comparison with controls. The profiles can be determined employing mass spectrometry.

Abstract: The disclosed methods address the identification and monitoring of cancer in a subject using serum peptide profiles. Such profiles allow the detection of the differential presence of certain serum peptide markers in comparison with controls. The profiles can be determined employing mass spectrometry.

Abstract: The disclosed methods address the identification and monitoring of cancer in a subject using serum peptide profiles. Such profiles allow the detection of the differential presence of certain serum peptide markers in comparison with controls. The profiles can be determined employing mass spectrometry.

Abstract: Many of the effects of nitric oxide are mediated by the direct modification of cysteine residues resulting in an adduct called a nitrosothiol. A method to detect proteins which contain nitrosothiols involves several steps. Nitrosylated cysteines are converted to tagged cysteines. Tagged proteins can then be detected, for example, by immunoblotting and/or can be purified by affinity chromatography. The method is applicable to the detection of S-nitrosylated proteins in cell lysates following in vitro S-nitrosylation, as well as to the detection of endogenous S-nitrosothiols in selected protein substrates.

Abstract: The present invention provides proteomic techniques that extend sensitive and quantitative analysis of proteins to post-translational modifications. Protein micro-arrays and/or multiplex coded-microbeads are used in combination with multilayered affinity interaction detection (MAID) methods that permit high throughput analysis of cellular protein modifications and functional protein interactions.

Abstract: Many of the effects of nitric oxide are mediated by the direct modification of cysteine residues resulting in an adduct called a nitrosothiol. A method to detect proteins which contain nitrosothiols involves several steps. Nitrosylated cysteines are converted to tagged cysteines. Tagged proteins can then be detected, for example, by immunoblotting and/or can be purified by affinity chromatography. The method is applicable to the detection of S-nitrosylated proteins in cell lysates following in vitro S-nitrosylation, as well as to the detection of endogenous S-nitrosothiols in selected protein substrates.

Abstract: A system for carrying out reactions that includes a small volume rotary selector valve having a plurality of peripheral ports and a small volume rotary switching valve, also having a plurality of peripheral ports, where the selector valve and switching valve are controlled by a computer. The rotary selector valve is connected by common port to a peripheral port of the rotary switching valve. The internal volumes of the rotary selector valve and rotary switching valves are 1.5 &mgr;l or less.

Abstract: Many of the effects of nitric oxide are mediated by the direct modification of cysteine residues resulting in an adduct called a nitrosothiol. A method to detect proteins which contain nitrosothiols involves several steps. Nitrosylated cysteines are converted to tagged cysteines. Tagged proteins can then be detected, for example, by immunoblotting and/or can be purified by affinity chromatography. The method is applicable to the detection of S-nitrosylated proteins in cell lysates following in vitro S-nitrosylation, as well as to the detection of endogenous S-nitrosothiols in selected protein substrates.

Abstract: System and process for performing complex reactions such as protein sequencing using small volumes and amounts of reagents, the system in part comprising the use of rotary type selector-switching value combinations.

Abstract: A protein complex containing 245 kDa and 35 kDa components, designated RAFT1 and RAFT2 (for Rapamycin And FKBP12 Target) interacts with FKBP12 in a rapamycin-dependent manner. This interaction has the pharmacological characteristics expected from the observed in vivo effects of rapamycin: it occurs at low nanomolar concentrations of rapamycin and is competed by excess FK506. Sequences (330 amino acids total) of tryptic peptides derived from the affinity purified 245 kDa RAFT1 reveals striking homologies to the predicted products of the yeast TOR genes, which were originally identified by mutations that confer rapamycin resistance in yeast. A RAFT1 cDNA was obtained and found to encode a 289 kDa protein (2550 amino acids) that is 43% and 39% identical to TOR2 and TOR1, respectively.

Abstract: A protein complex containing 245 kDa and 35 kDa components, designated RAFT1 and RAFT2 (for Rapamycin And FKBP12 Target) interacts with FKBP12 in a rapamycin-dependent manner. This interaction has the pharmacological characteristics expected from the observed in vivo effects of rapamycin: it occurs at low nanomolar concentrations of rapamycin and is competed by excess FK506. Sequences (330 amino acids total) of tryptic peptides derived from the affinity purified 245 kDa RAFT1 reveals striking homologies to the predicted products of the yeast TOR genes, which were originally identified by mutations that confer rapamycin resistance in yeast. A RAFT1 cDNA was obtained and found to encode a 289 kDa protein (2550 amino acids) that is 43% and 39% identical to TOR2 and TOR1, respectively.

Abstract: The present invention presents three B. burgdorferi membrane proteins: Oms28, Oms45, and Oms66, each of about 28, 45, and 66 kDa respectively; and with average single channel conductances of about 0.6, 0.22, and 9.7 nS, respectively. Also disclosed are the methods for purifying these proteins from B. burgdorferi, methods for producing antibodies to these proteins, and the resulting antibodies. These proteins and their immunogenic fragments, and antibodies capable of binding to them are useful for inducing an immune response to pathogenic B. burgdorferi as well as providing a diagnostic target for Lyme disease. Further disclosed are the nucleotide and amino acid sequences, the cloning of the genes encoding the proteins and their recombinant proteins, and methods for obtaining the foregoing. Other B. burgdorferi outer membrane spanning proteins (Oms) obtainable by the isolation and purification methods of the present invention.

Abstract: This invention provides a purified polypeptide having antibacterial activity comprising a first sequence Pro-Arg-Pro-Pro-His-Pro-Arg-X1, wherein X1 is Ile or Leu; and a second sequence X2-Pro-X3-X4-X5-Pro, wherein X2 is Arg or Lys, X3 is Thr, Gln or Arg, X4 is Tyr, Gln or Pro, and X5 is Val or Ala, the second sequence is N-terminal to the first sequence. This invention also provides a purified polypeptide having antibacterial activity comprising: a first sequence, at least seven amino acid residues are the same as Pro-Arg-Pro-Pro-His-Pro-Arg-X1, wherein X1 is Ile or Leu; a second sequence X2-Pro-X3-X4X5-Pro, wherein X2 is Arg or Lys, X3 is Thr, Gln or Arg, X4 is Tyr, Gln or Pro, and X5 is Val or Ala, the second sequence is N-terminal to the first sequence; and a third sequence comprising at least five amino acid residues, at least one-third of the residues are Pro, the third sequence is N-terminal to the second sequence.

Abstract: New bactericidal and/or bacteriostatic, thermostable peptides which are isolated from hemolymph of immune honeybees and which are distinct from lysozymes, attacins, cecropins, diptericins and magainins. The peptides feature at least the 10 C-terminal amino acids of the following peptide:H.sub.2 N-Gly-Asn-Asn-Arg-Pro-X-Tyr-Ile-Pro-Gln-Pro-Arg-Pro-Pro-His-Pro-Arg-Z-OHin whichX is a valyl or isoleucyl residue andZ is a leucyl or isoleucyl residue.