The present invention provides for compounds and methods for the detection and follow-up of Fabry disease (FD). In particular, the present invention relates to a method for detecting or diagnosing FD in a subject, comprising detecting globotriaosylceramide (Gb3) deposits in biomaterial obtained from said subject. The present invention also provides for a method for treatment monitoring of FD in a subject. Further, the present invention relates to the use of a Gb3-specific natural ligand for the detection of Gb3 deposits in biomaterial. Also provided is a kit for detecting Gb3 deposits in biomaterial obtained from a subject.

Provided is a high-accuracy analysis method utilizing an enzyme-lined immunoassay. The presence of an analyte 3 can be detected or the abundance of the analyte 3 can be analyzed by: bonding an antibody 5 that is capable of specifically bonding to the analyte 3 immobilized on a solid phase 1 and has an enzyme 7 bonded thereto; then decomposing an enzyme substrate 8, which can generate decomposition products capable of being detected easily with a mass spectrometry, with the enzyme 7 bonded to the antibody 5; and then analyzing the decomposition products 9 and 10 with a mass spectrometry.

Provided are in vitro and in vivo methods for determining whether a patient with Fabry disease will respond to treatment with a specific pharmacological chaperone.

Provided are in vitro and in vivo methods for determining whether a patient with Fabry disease will respond to treatment with a specific pharmacological chaperone.

Provided is a high-accuracy analysis method utilizing an enzyme-lined immunoassay. The presence of an analyte 3 can be detected or the abundance of the analyte 3 can be analyzed by: bonding an antibody 5 that is capable of specifically bonding to the analyte 3 immobilized on a solid phase 1 and has an enzyme 7 bonded thereto; then decomposing an enzyme substrate 8, which can generate decomposition products capable of being detected easily with a mass spectrometry, with the enzyme 7 bonded to the antibody 5; and then analyzing the decomposition products 9 and 10 with a mass spectrometry.

The present invention provides methods to determine whether a patient with a lysosomal storage disorder will benefit from treatment with a specific pharmacological chaperone. The present invention exemplifies an in vitro method for determining α-galactosidase A responsiveness to a pharmacological chaperone such as 1-deoxygalactonojirimycin in a cell line expressing a mutant from of α-galactosidase A. The invention also provides a method for diagnosing Fabry disease in patients suspected of having Fabry disease.

The present invention provides methods to determine whether a patient with a lysosomal storage disorder will benefit from treatment with a specific pharmacological chaperone. The present invention exemplifies an in vitro method for determining α-galactosidase A responsiveness to a pharmacological chaperone such as 1-deoxygalactonojirimycin in a cell line expressing a mutant from of α-galactosidase A. The invention also provides a method for diagnosing Fabry disease in patients suspected of having Fabry disease.

The present invention provides methods to determine whether a patient with a lysosomal storage disorder will benefit from treatment with a specific pharmacological chaperone. The present invention exemplifies an in vitro method for determining -galactosidase A responsiveness to a pharmacological chaperone such as 1-deoxygalactonojirimycin in a cell line expressing a mutant from of -galactosidase A. The invention also provides a method for diagnosing Fabry disease in patients suspected of having Fabry disease.

Disclosed is an analyzing method, for analyzing a blood specimen, which includes: mixing a blood specimen and a thrombin-containing reagent to coagulate the blood specimen, and obtaining a coagulation waveform; obtaining a value of a parameter concerning differentiation of the coagulation waveform, based on the coagulation waveform; and obtaining information concerning an amount of antigen of fibrinogen based on the obtained value of the parameter.

The present invention provides a method for determining carbonyl ratio and/or concentration of oxidized nanofibrillar cellulose in a sample. In accordance with the invention oxidized nanofibrillar cellulose comprised in the sample is enzymatically hydrolyzed into oxidized cellobioses which are specific markers to oxidized nanofibrillar cellulose. The cellobioses may be then analyzed and quantified to reveal the amount of oxidized nanofibrillar cellulose in the sample. A method for determining the concentration of oxidized nanofibrillar cellulose in a sample comprises steps of providing an analytical sample of material comprising oxidized nanofibrillar cellulose; hydrolyzing the analytical sample to breakdown products of oxidized nanofibrillar cellulose in presence of one or more enzymes; subjecting the breakdown products to a separation analysis to reveal the relative amounts of the breakdown products; and determining the concentration of oxidized nanofibrillar cellu-lose.