Abstract: The present invention provides, as a novel diagnosis marker for type 1 diabetes mellitus, a type 1 diabetes mellitus diagnostic composition comprising alanyl-tRNA synthetase, glycyl-tRNA synthetase, asparaginyl-tRNA synthetase, or tryptophanyl-tRNA synthetase, a diagnostic kit comprising the same, and a diagnostic method using the same. The composition, the kit, and the method, according to the present invention, may be used for early diagnosis and confirmed diagnosis of type 1 diabetes mellitus because type 1 diabetes mellitus can be easily diagnosed from a patient sample.

Abstract: By detecting an antibody which immunologically reacts with amylase ?2-A in a sample, AIP or FT1DM is examined or the possibility of developing FT1DM is determined. For instance, detection of this antibody is carried out by an immunological method using an antigen which immunologically reacts with this antibody. The antigen is preferably a partial fragment containing the amino acid sequence of amino acid numbers 299 to 511 of human amylase ?2-A (SEQ ID NO: 1).

Abstract: The present invention relates to a specific C-peptide assay method which can eliminate all interference due to proinsulin and its intermediates, in particular des-31,32-proinsulin and/or des-64,65-proinsulin. It also relates to antibodies for carrying out this assay.

Abstract: A method for judging an autoimmune disease by detecting the existence of an anti-Reg protein autoantibody in a specimen; and a method for judging insulin-dependent or non-insulin-dependent diabetes mellitus. A method for detecting an anti-Reg protein autoantibody by bringing into a specimen into contact with an antigen component and detecting the formation of an immune complex. A reagent for diagnosing autoimmune disease which contain an antigen component capable of binding specifically to the anti-Reg protein autoantibody; and a reagent for diagnosing insulin-dependent or non-insulin-dependent diabetes mellitus.

Abstract: The method and compositions of this invention provide an effective and reliable substitute for the currently employed ICA assay for diabetes. By providing a method for detecting autoantibodies to both GAD65 and IA-2 auto-antigens, the method provides a chemical assay which has improved reliability. In addition, these antigens may be employed in therapeutic regimens aimed at achieving immune tolerance and therefore amelioration of the clinical condition.

Abstract: Pancreatic disease can be diagnosed by assaying a patient's body fluid such as serum or urine, for pancreatic activation peptides (PAP) released from zymogens by proteolytic activation. Particularly useful are peptides having C-terminal D.sub.4 K sequences. The method uses polyclonal or monoclonal antibodies generated and selected for C-terminal specificity on PAP so that the tests only report free PAP not parent zymogen. Also described are peptides and antibodies labelled with revealing agents and/or immobilised on solid supports and their use in diagnostic assays and kits. In pancreatic disease the tests distinguish necrotising from oedematous acute pancreatitis and permit severity prediction and monitoring as well as diagnosing chronic pancreatitis in exacerbation.

Abstract: A novel growth factor (BTC-GF) was purified from the conditioned medium of pancreatic beta tumor cells initially derived from transgenic mice (RIPI-Tag2). The purification scheme included BioRex 70 chromatography, phenyl-Sepharose chromatography, TSL-GEL heparin FPLC and C4 reverse phase HPLC. The peptide also stimulated proliferation of bovine smooth muscle cells. It was not inactivated by boiling, by 10 mM dithiothreitol or by exposure to 1M acetic acid. Biological activity of BTC-GF was recovered from a single band of protein which had a molecular weight of 32,000 on SDS-PAGE.

Abstract: This invention is directed to antibodies which react with human islet amyloid polypeptide and which do not significantly react with insulin or calcitonin gene-related peptides. Preparations of antibodies are provided which bind to islet amyloid polypeptide (IAPP) which is substantially free of islet amyloid, and when isolated from humans, has the following amino acid sequence in positions 1-37:Lys-Cys-Asn-Thr-Ala-Thr-Cys-Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val- His-Ser-Ser-Asn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-Thr-Asn-Val-Gly- Ser-Asn-Thr-Tyr.

Abstract: A novel growth factor (BTC-CG) was purified from the conditioned medium of pancreatic beta tumor cells initially derived from transgenic mice (RIPl-Tag2). The purification scheme included BioRex 70 chromatography, phenyl-Sepharose chromatography, TSL-GEL heparin FPLC and C4 reverse phase HPLC. The peptide also stimulated proliferation of bovine smooth muscle cells. It was not inactivated by boiling, by 10 mM dithiothreitol or by exposure to IM acetic acid. Biological activity of BTC-GF was recovered from a single band of protein which had a molecular weight of 2,000 on SDS-PAGE. The Partial N-terminal amino acid sequence of this protein was determined with an ABI 470A protein sequencer as: Asp-Gly-[X]-Thr-[X]-Arg-Thr-Pro-Glu-[X]-Asn-Gly.

Abstract: DNA sequences encoding modified varieties of human PSTI possessing excellent stability in terms of decreased susceptibility to decomposition by proteolytic enzymes such as trypsin, as compared with natural human PSTI, as well as the modified varieties of human PSTI obtained by the expression of the DNA sequences.

Abstract: Subunits of the full length 37 amino acid residue human Islet Amyloid Polypeptide, and feline Islet Amyloid Polypeptide essentially free of unpolymerized amyloid are provided. Islet Amyloid Polypeptide (IAPP) may be isolated and purified from amyloid fibrils using depolymerizing agent and chromatographic techniques. The sequences of the purified Islet Amyloid Polypeptides have been determined Purified Islet Amyloid Polypeptides are suitable for induction of anti-IAPP antibodies.

Abstract: Antibodies specific for pancreatic alpha-amylase and methods for their production are described. These antibodies may be used for the detection and quantification of pancreatic alpha-amylase in biological fluids, tissue extracts, or extracts of stains of biological fluids.