426 PATENT ABSTRACTS

hybridization event. The assay can be used for a assay is directly proportional to the concentra- variety of laboratory and clinical purposes and is tion of functional HMWK, may be determined automatable, by functional assay using an appropriate factor

XIa substrate.

4 8 8 2 2 7 1

P R O C E S S F O R P R E P A R A T I O N O F 4 8 8 2 2 7 5

H I G H M O L E C U L A R W E I G H T M E T H O D O F P U R I F Y I N G C E L L - A S S O C I A T E D P R O T E I N O F E N D O T H E L I A L C E L L G R O W T H C A M P Y L O B A C T E R P Y L O R I A N D F A C T O R S U S I N G I M M O B I L I Z E D

U S E F O R S E R O L O G I C A L H E P A R I N D E T E C T I O N O F

C A M P Y L O B A C T E R P Y L O R I I N F E C T I O N Michael Klagsbrun assigned to The Children's

Medical Center Corporation

Dolores G Evans, Doyle Evans, David Y Endothelial cell growth factor (ECG) from Graham assigned to Baylor College of Medicine various sources possesses a strong and specific

affinity for heparin. This strong affinity of ECG An antigen for the detection of Compylobacter for heaprin enables removal of undesired im- pylori infections and an assay for the serological purities from a mixture comprising ECG by: (a) detection of Campylobacter pylori. The antigen contacting immobilized heparin with the mix- includes high molecular weight cell-associated ture to form a heparin-ECG complex; (b) proteins purified from Campylobacter pylori, separating uncomplexed mixture from the com- The antigen can be used in a variety of assays in- plex; and (c) contacting the complex with a salt cluding radioimmunoassay, ELISA, latex ag- solution of a salt concentration and pH effective glutination, complement fixation, and indirect to separate the ECG from the heparin. The resul- hemagglutination. Furthermore, the antigens ting purified ECG (or fragment thereof) is useful can be combined with a solid support in kit form. in therapeutics and as an additive for cell cul-

turing. The purified ECG is also useful to raise antibodies that are used in therapeutics and in ECG immunoassays.

4 8 8 2 2 7 2

H I G H M O L E C U L A R W E I G H T K I N I N O G E N A S S A Y

4 8 8 2 2 8 0

Cheryl F Scott, Robert W Colman assigned to Temple University - of the Commonwealth Sys- U R I C A S E A N D A M E T H O D F O R tern of Higher Education T H E P R E P A R A T I O N T H E R E O F

An assay for functional high molecular weight Masachika Takashio, Takahide Chikano, kininogen in plasma is provided. A plasma sam- Minoru Kamimura, Yaizu, Japan assigned to ple of unknown functional high molecular Sapporo Breweries Limited kininogen content is treated to inactivate plasma protease inhibitors and kallikrein, and is ap- Different from conventional uricase products, propriately neutralized and diluted. Exogenous the uricase of the present invention has out- factor XIIa and factor XI are added to the sam- standingly high thermal stability and is active in pie to form a reaction mixture which is incubated a wide range of pH from 5 to 10 for the oxidative with a contact-activating surface. The con- decomposition of uric acid undertaken in clinical centrations of'factor Xlla and factor XI in the analysis. The uricase of the invention is pro- reaction mixture are selected such that the con- duced microbiologically by a thermophilic centration of functional high molecular weight microorganism belonging to the genus of Bacil- kininogen in the sample is rate-limiting in the lus and especially named as Bacillus sp. TB-90 HMWK-mediated activation of factor XI by which is a novel species distinguishable from any factor XIIa. The amount of factor Xla generated of the microorganisms belonging to the genus of in the sample, which under the conditions of the Bacillus.