Abstract: The present invention provides an immunoassay method for screening for gram negative sepsis in a subject, in which the concentration of extracellular BPI in a plasma sample from the subject is determined and compared with a standard concentration of BPI indicative of gram negative sepsis.
Type:
Grant
Filed:
December 29, 1993
Date of Patent:
November 14, 1995
Assignee:
XOMA Corporation
Inventors:
Mark L. White, Stephen F. Carroll, Jeremy K.-k. Ma
Abstract: The present invention provides a method for quantifying the presence of extracellular BPI in body fluids including blood in a subject comprising conducting a BPI immunoassay on plasma obtained from said subject.
Type:
Grant
Filed:
September 22, 1993
Date of Patent:
November 14, 1995
Assignee:
XOMA Corporation
Inventors:
Mark L. White, Stephen F. Carroll, Jeremy K. Ma
Abstract: A substantially pure receptor with binding activity for rhinoviruses of the small receptor group is disclosed, which has the following characteristics:(a) a molecular weight of 120 kD on a polyacrylamide gel in the presence of SDS;(b) a sedimentation constant, determined by sucrose gradient centrifugation in the presence of detergents, corresponding to about 28.4 S;(c) is bound by Lens culinaris lectin;(d) is not bound by heparin-sepharose;(e) is bound irreversibly to an anion exchanger;(f) has binding activity which is insensitive to neuraminidase;(g) consists of sub-units connected by intermolecular disulfide bridges;(h) shows no binding activity to rhinoviruses in the presence of EDTA; and(i) has a binding activity to rhinoviruses which is only slightly influenced by iodoacetamide.A receptor subunit of the above-described receptor, produced by complete reduction of said receptor, is also disclosed.
Type:
Grant
Filed:
January 19, 1994
Date of Patent:
September 5, 1995
Assignee:
Boehringer Ingelheim International GmbH
Inventors:
Dieter Blaas, Ernst Kuechler, Harald Mischak, Christoph Neubauer
Abstract: This invention is directed to kits for the detection of human islet amyloid polypeptide (IAPP) comprising (a) purified preparations of antibodies which react specifically with insulin or calcitonin gene-related peptides and (b) a preselected amount of human islet amyloid polypeptide which is essentially free of islet amyloid, which polypeptide is one subunit of islet amyloid and which is prepared by depolymerizing human islet amyloid; or a preselected amount of human islet amyloid polypeptide which is essentially free of islet amyloid and has the amino acid sequence: lys-cys-Asn-Thr-Ala-Thr-Cys-Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val-His-Se r-Ser-Asn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-Thr-Asn-Val-Gly-Ser-Asn-Thr-Tyr.
Abstract: At the initial diagnosis of sepsis (6-24 h before the development of ARDS), serum manganese superoxide dismutase (MnSOD) levels and catalase activities are increased in septic patients who subsequently developed ARDS compared to septic patients who did not develop ARDS. Increases in MnSOD and catalase may be used to predict the occurrence of ARDS in septic patients with the same sensitivity, specificity and efficiency as parallel assessments of serum lactate dehydrogenase (LDH) and Factor VIII levels. Evaluation of serum MnSOD and catalase as well as these other accessible markers facilitates identification of subsets of patients and allows prospective treatment of septic patients who are destined to develop ARDS.
Abstract: Disclosed is a method for the determination of urinary protein and creatinine in a single reaction vessel using a continuous process. The method involves adjusting the pH to a level suitable for carrying out an immuno assay for the protein and making such a determination by an immuno agglutination technique. Raising the pH to a level suitable for determining the creatinine quickly dissipates the cloudiness caused by the agglutination reaction, so that the creatinine determination can be carried out without delay.
Abstract: The present invention relates to a process of preparing a sandwich immunoassay of NAG, which comprises (1) reacting NAG with an immobilized anti-NAG monoclonal antibody and a labeled anti-NAG monoclonal antibody to form a complex of immobilized antibody-NAG-labeled antibody and (2) detecting the activity of said reacted and unreacted labeled anti-NAG antibody.This sandwich immunoassay is useful for diagnosis of renal disease, hepatitis, leukemia, and other such diseases. It also allows the direct and specific detection of NAG isozymes B and I in urine and blood.