An objective is to provide a marker that enables a diabetic complication to be examined. There is provided the marker for examining a diabetic complication, comprising a compound represented by the following Formula (1), or a salt thereof.

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Provided are an analytical method and apparatus using fingerprints on the basis of the types and expression levels of expressed trace proteins and/or peptides contained in living tissue and/or biological fluid. The present invention relates to a method and apparatus for analyzing the status of living tissue and/or biological fluid by binding a specific fluorogenic reagent (such as DAABD-Cl) to expressed trace proteins and/or peptides contained in living tissue and/or biological fluid without degradation treatment followed by precisely detecting and separating by nano-liquid chromatography, and subsequently continuously and quantitatively measuring the separated and purified fluorescent labelled proteins and/or peptides using a fluorescence detector. The use of a nano-liquid chromatograph having a fluorescence detector makes it possible to obtain profiles of expressed trace proteins and/or peptides contained in living tissue and/or biological fluid.

Disclosed are methods and systems for measuring serotonin in a sample using liquid chromatography and mass spectrometry.

The present invention relates to a method for determining the distinctive nutritional requirements of a patient with specific nutritional needs and providing a composition meeting the distinctive nutritional requirements of said patient.

A method of ionising a sample is disclosed comprising nebulising a sample which includes monoclonal antibody (mAb) molecules. A stream of monoclonal antibody droplets or charged droplets is directed so as to impact upon a target or electrode so as to form intact parent monoclonal antibody ions, intact minus light chain parent monoclonal antibody ions or light chain (LC) fragment monoclonal antibody ions.

Disclosed is a novel means for accurate qualitative and quantitative analyses for each N-glycosylation site. The method of analyzing N-linked sugar chain(s) of glycoprotein according to the present invention comprises: treating a part of a glycopeptide-containing sample to be analyzed with endo--N-acetylglucosaminidases to cleave off sugar chains while leaving one GlcNAc of the chitobiose core on the Asn at the N-glycosylation site; subjecting the obtained sugar chain-cleaved sample to preliminary liquid chromatography/mass spectrometry; predicting the retention time of the glycopeptide of interest and the mass-to-charge ratio (m/z) of the precursor ion in main analysis based on the results of the preliminary liquid chromatography/mass spectrometry; and carrying out the main analysis. By this method, the binding sites and structures of N-linked sugar chains in a glycoprotein can be analyzed. By using the sugar chain-cleaved sample as an internal standard in the main analysis, quantitative analysis of sugar chains at each glycosylation site also becomes possible.

The present invention relates to the use of HTRA1 mRNA antagonists in the treatment of eye disorders, such as macular degeneration, and the use of an HTRA1 levels in the aqueous and vitreous humor as a diagnostic biomarker for the suitability of treatment of a subject with an HTRA1 mRNA antagonist.

Methods and kits for detecting and/or quantitating target proteins in biological samples. In particular, the method comprises capture and immobilization of the target protein, protein denaturation, proteolytic digestion, and analysis using a mass spectrometry-based technique.

The invention relates to peptide mass fingerprinting technique for the proteins such as Human insulin and insulin analogs. The insulin analogues can vary at least by one amino acid, which is elusive to distinguish by currently available analytical methods. The invention further allows sequence confirmation of the peptide wherein the run time of the method is forty minutes. This method could be applied for molecules up to 50 kDa.

Real-time search (RTS) for mass spectrometry is described. In one aspect, a mass spectrometer can identify a candidate peptide for a product ion spectrum by searching a mass spectral database. While executing the search of the mass spectral database, the elapsed search time can be monitored. If the elapsed search time of the identification of the candidate peptide is completed before reaching a maximum value, then the mass spectrometer can perform further actions.