Abstract: An aminopeptidase which is a component of GLUT4-containing vesicles in the natural state, and which cleaves insulin. The claimed protein has an apparent molecular weight of approximately 110 kD in its deglycosylated form and a predicted molecular weight of 117,239 Daltons. It includes the amino acid sequences Phe-Ala-Ala-Thr-Gln-Phe-Glu-Pro-Leu-Ala-Ala (SEQ ID NO: 1) and Ile-Leu-Gln-Asn-Gln-Ile-Gln-Gln-Gln-Thr-Arg-Thr-Asp-Glu-Gly-Xaa-Pro-Xaa-Me t (SEQ ID NO: 2, and reacts with antibodies produced against the peptide identified as (SEQ ID NO: 1). It is encoded by the cDNA of FIG. 20 (SEQ. ID NOs. 15 and 16) and is essentially the protein sequence therein described. Modulators of the activity of the aminopeptidase and a method for treating syndromes of insulin resistance, including diabetes, by administration of such a modulator are also claimed.

Abstract: An aminopeptidase which is a component of GLUT4-containing vesicles in the natural state, and which cleaves insulin. The claimed protein has a molecular weight of approximately 110 kD in its deglycosylated form. It includes the amino acid sequences Phe-Ala-Ala-Thr-Gln-Phe-Glu-Pro-Leu-Ala-Ala [SEQ ID NO: 1] and Ile-Leu-Gln-Asn-Gln-Ile-Gln-Gln-Gln-Thr-Arg-Thr-Asp-Glu-Gly-Xaa-Pro-Xaa-Me t [SEQ ID NO: 2], and reacts with antibodies produced against the peptide identified as [SEQ ID NO: 1]. Modulators of the activity of the aminopeptidase and a method for treating syndromes of insulin resistance, including diabetes, by administration of such a modulator are also claimed.

Abstract: Methods and apparatus for moving fuel bundles in a reactor pressure vessel (RPV) of a nuclear reactor are described. In one embodiment of the apparatus, a support tube facilitates the positioning of a multiple channeled magazine within the RPV, especially at locations adjacent fuel bundles. In the one embodiment, the support tube extends in the reactor pressure vessel into the area above the top guide. A magazine assembly is coupled to the support tube, and includes a magazine having a plurality of fuel bundle receiving channels. The magazine extends from the support tube so that it is adjacent the fuel bundles and the top guide. Grapples extend through the magazine channels, engage the fuel bundles, and retract the bundles into the magazine channels. The magazine and support tube, and thus the bundles, are then moved.

Abstract: Monoclonal antibodies specific for the glycosylated lysine residue at position 525 in glycoalbumin and a method for producing such antibodies. The monoclonal antibodies are useful as reagents in immunoassays for the specific determination of glycoalbumin in human blood samples which is indicative of the severity of the diabetic condition. The monoclonal antibodies are secreted by hybridomas obtained by fusing a myeloma cell with a lymphocyte that has been taken from an animal, usually a mouse, immunized with a peptide immunogen and which produces antibody to the lysine 525 residue in glycoalbumin. The synthetic peptide immunogen comprises a peptide residue which includes an .epsilon.-amino glucosylated lysine and an adjacent amino acid sequence in which at least one of the amino acid units is in a position corresponding to the peptide sequence of human albumin adjacent to lysine 525, the glycosylated peptide residue being linked to an immunogenic carrier.

Abstract: Diagnosis of insulin-dependent (Type I) diabetes mellitus (IDDM) by contacting a blood sample from a patient with an immunoreagent comprising epitopes of two or more of glutamic acid decarboxylase (GAD) and the pancreatic islet cell antigens referred to as ICA512 and ICA12. Binding of antibodies present in the blood sample with one or more of such epitopes correlates with IDDM or a potential for developing IDDM. In clinical testing, about 80 percent of sera from newly diagnosed IDDM patients react positively with at least one epitope in a GAD/ICA512 panel. Reactivity with the GAD/ICA512/ICA12 panel is between about 80 and 90 percent. The method is useful in screening patients for pre-IDDM, for distinguishing IDDM from Type II diabetes, and for monitoring therapy.

Abstract: Monoclonal antibodies specific for the glycosylated lysine residue at position 525 in glycoalbumin and a method for producing such antibodies. The monoclonal antibodies are useful as reagents in immunoassays for the specific determination of glycoalbumin in human blood samples which is indicative of the severity of the diabetic condition. The monoclonal antibodies are secreted by hybridomas obtained by fusing a myeloma cell with a lymphocyte that has been taken from an animal, usually a mouse, immunized with a peptide immunogen and which produces antibody to the lysine 525 residue in glycoalbumin. The synthetic peptide immunogen comprises a peptide residue which includes an .epsilon.-amino glucosylated lysine and an adjacent amino acid sequence in which at least one of the amino acid units is in a position corresponding to the peptide sequence of human albumin adjacent to lysine 525, the glycosylated peptide residue being linked to an immunogenic carrier.

Abstract: A method for determining the adequacy of a cervical or urethral test specimen collected for an immunological assay to detect the presence of Chlamydia trachomatis. Cells present in the specimen are disrupted to expose a substance present in or on C. triachomatis that is detectable by immunological reaction. In order to determine if the test specimen contains an adequate amount of the cervical or urethral cell type that serves as a host cell for C. trachomatis, the disrupted specimen is also reacted with an immunological reagent that produces a detectable complex upon specific binding with a substance present in or on columnar epithelial cells. The present invention therefore provides a control reaction that verifies the adequacy of the collected test specimen and thereby increases the confidence that a negative test result for the presence of Chlamydia indicates the absence of a C. trachomatis infection in the patient.

Abstract: A method is provided of making an oligonucleotide which comprises hybridizing (a) a shorter fragment of the desired oligonucleotide with (b) a nucleic acid fragment longer than (a) and complementary to the desired oligonucleotide, one of (a) and (b) is linked to an organic radical which differentiates its physical properties relative to the other of (a) and (b), contacting the hybridized material with an enzyme and nucleoside triphosphates whereby the shorter fragment is extended in one direction until it is substantially coterminal with the complementary nucleic acid fragment, denaturing the hybridized material and separating lengthened (a) from (b).

Abstract: A nucleic acid detection probe comprising a hybridizable single stranded portion of nucleic acid connected with a non-hybridizable, single or double stranded nucleic acid portion, the non-hybridizable portion preferably including a recognition site for binding by a particular protein. Such recognition site can be a region of singly or doubly stranded nucleic acid specific for a particular nucleic acid binding protein such as lac repressor protein or can be a modified nucleic acid region such as a unique antigenic determinant introduced by interaction of the region with a modifier compound such as an intercalating agent or a platinum-containing ligand. The probe-binding protein can be labeled for ease of detection and in the case of an antigenic determinant binding site can be labeled antibody.

Abstract: A protein is covalently coupled to a 3'terminal end of a nucleic acid which carries several labels. In an assay the protein will specifically recognize some component of a test system; in an immunoassay the protein can be Protein A which will recognize the FC portion of IgG which is bound to an unknown antigen if present in the test sample.

Abstract: Monoclonal antibodies specific for the glucosylated N-terminal peptide residue in Hb A.sub.1c, a method for producing such antibodies, hybridoma cell lines secreting such antibodies and a method for their production, and immunoassay methods and reagent systems using such antibodies for the determination of Hb A.sub.1c in human blood samples. The monoclonal antibodies are secreted by hybridomas obtained from the fusion of a myeloma cell and a lymphocyte which has been taken from an animal, preferably a mouse, immunized with a synthetic peptide immunogen and which produces antibody specific for the glucosylated N-terminal peptide residue in Hb A.sub.1c. The synthetic peptide immunogen comprises an N-terminal plucosylated peptide residue having at least 2 amino acid units corresponding to the N-terminus of the beta-subunit of human hemoglobin and an immunogenic carrier to which the glucosylated peptide residue is linked.

Abstract: A detection probe comprising a hybridizable single stranded portion of nucleic acid connected with a non-hybridizable, single or double stranded nucleic acid portion, the non-hybridizable portion preferably including a recognition site for a particular protein.

Abstract: Binding of a particular protein by an antibody reagent involving denaturation of the protein and use of an antibody reagent specific for binding a linear peptide epitope therein. Denaturation by chemical or physical means effectively exposes or enhances the exposure of the linear peptide epitope for binding by the antibody reagent which is preferably raised against a synthetic peptide immunogen. The technique is particularly useful in performing immunoassays for protein analytes, such as a glycosylated protein, in aqueous test samples.

Abstract: Monoclonal antibodies specific for the glucosylated N-terminal peptide residue in Hb A.sub.1c, a method for producing such antibodies, hybridoma cell lines secreting such antibodies and a method for their production, and immunoassay methods and reagent systems using such antibodies for the determination of Hb A.sub.1c in human blood samples. The monoclonal antibodies are secreted by hybridomas obtained from the fusion of a myeloma cell and a lymphocyte which has been taken from an animal, preferably a mouse, immunized with a synthetic peptide immunogen and which produces antibody specific for the glucosylated N-terminal peptide residue in Hb A.sub.1c. The synthetic peptide immunogen comprises an N-terminal glucosylated peptide residue having at least 2 amino acid units corresponding to the N-terminus of the beta-subunit of human hemoglobin and an immunogenic carrier to which the glucosylated peptide residue is linked.