Johns Hopkins University

Memorial Sloan Kettering Cancer Center

University of California

Sloan-kettering Institute for Cancer Research

Plant Genetic Systems N.v.

Paul J Tempst

Solomon H Snyder

Hediye Erdjument-Bromage

Samie R Jaffrey

Cheryl I Champion

Peter Casteels

David R Blanco

James N Miller

Michael A Lovett

Christopher D Ferris

Mary Lui

David M Sabatini

Mark Albert Vaeck

Ellen S Shang

Tajib A Mirzabekov

Michael Powell

Bruce L Kagan

Denise M Foley

Josep Villanueva

Frans Jacobs

Jonathan T Skare

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.

Methods of detection of cancer using peptide profiles

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.

Method for assaying protein nitrosylation

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.

System and process for microfluidics-based automated chemistry

A protein complex containing 245 kDa and 35 kDa components, designated RAFT1 and RAFT2 (for apamycin nd KBP12 arget) 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.

Mammalian proteins that bind to FKBP12 in a rapamycin-dependent fashion

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.

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.

Borrelia burgdorferi outer membrane proteins

Antigenic rare outer membrane proteins of Spirochaetaceae are obtained from organisms extracted from infected tissue by a novel process of isolation utilizing a discontinuous Ficoll gradient separation, release of outer membrane in a low isotonic and low pH buffer and identification of outer membrane by use of a lipid soluble dye. Four antigenic rare outer membrane proteins of T. pallidum subsp. pallidum useful in diagnosis and prophylaxis of syphilis are provided. Also provided are the amino acid sequences of two rare outer membrane proteins of T. pallidum subsp. pallidum, called TROMP 1 and TROMP 2, and the nucleotide sequences encoding them.

Nucleotide sequences of T. pallidum rare outer membrane protein

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.

Apidaecin-type peptide antibiotics with improved activities and/or

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:

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New York, NY, United States of America

Paul J Tempst