604
PATENT ABSTRACTS
Sezary cell hybridomas which secrete MCF and thereby provide a ready source for MCF isolation and purification. Sezary's Syndrome is a leukemic proliferation o f O K T 4 + lymphocytes. Sezary cells were isolated by differential centrifugation and fused to CEM.8azar/.C, an HGPRTase lacking clone of CEM. The hybrid cells were studied for their ability to produce soluble mediators of human monocyte cytotoxicity. The product of a single clone, FtF3, which bore the surface phenotype of Sezary cells, was characterized. Monocyte cytotoxicity inducing factor was found to be stable at pH 2 for one hour, unlike interferon-gamma, and was found to be more heat stable as well. Moreover, treatment of M C F with antisera to interferons gamma, alpha, or a combination of gamma and alpha failed to neutralize its biologic activity. M C F binds to Matrex Gel Red A. MCF elutedfrom this dye-ligand was found to have an apparent molecular weight of I 1,500 Daltons by gel filtration and 14,700 Daltons by SDSpolyacrylamide gel electrophoresis (SDSPAGE). A molecular weight of 29,000 daltons was found by use of SDS-PAGE in a second species of MCF produced under serum-free conditions.
5286483 50 K I L O D A L T O N
ANTIGEN OBTAINED FROM THE INTRAERYTHROCYTIC PHASE OF PLASMODIUM FALCIPARUM
5286484 NUCLEOTIDE SEQUENCE CODING FOR AN OUTER M E M B R A N E P R O T E I N FROM NE1SSERIA MEN1NGITIDIS AND USE OF SAID PROTEIN IN VACCINE PREPARATIONS Silva Rodriquez, Selman H Sosa, Guillen Nieto, Saturnino H Martinez, R F MasoJulio, Lidia I N Perez, Juan M Grillo, Vivian M Cordova, Sonia G Blanco, Beatriz T Santos, Valle Rosales Jesus A del, Evelin Menendez, Anabel A Acosta, Edelgis C Rodriquez, Silian Leon, Alexis M Lasa, Ciudad de la Habana, Cuba assigned to Centro de lngenieria Genetica y Biotecnologia The present invention is concerned with a method for the isolation ofa nucleotide sequence which codes for a protein having a molecular weight of about 64,000 daltons, which is located on the outer membrane of N. meningitidis, as well as with the recombinant DNA obtained therefrom, which is used for the transformation of a host microorganism. The technical object pursued with the invention is the identification o f a nucleotide sequence coding for a highly conserved and common protein for the majority of pathogenic Neisseria strains, the production of this protein with a high level of purity and in commercially useful amounts using the recombinant way, so that it can be used in diagnostic methods and vaccine preparations with a broad immunoprotection spectrum.
Alain Vernes, Francois J Dubrometz, Bernard Fortier, Patrick Deplace, 59 800 Little, France The invention concerns antigens from the intraerythrocytic phase of Plasmodium falciparum, namely: a protein of 50 kDa with an isoelectric point of 5.5 and a protein of 65 kDa separated by electrophoresis in reducing conditions into two polypeptides of 47 and 18 kDa, both appearing in the serum of patients infected by Plasmodium falciparum or in the culture medium of this microorganism during its intraerythroeytic phase, as well as a protein of 126 kDa synthesized during the nuclear multiplication phase during schizogony and localized on the periphery of the schizonts at the parasitophore vacuole level, precursor of the 50 kDa and 65 kDa proteins. Application of these proteins in the preparation of vaccines against malaria, and monoclonal antibodies corresponding to the assay of the antibodies of an immunized subject and assay of the antigens aCcording to the invention during an attack of malaria.
5286487 COVALENT
ANGIOGENIN/RNASE HYBRIDS
Bert L Vallee, Michael D Bond assigned to President and Fellows of Harvard College Regional mutagenesis of a gene for angiogenin to produce DNA sequences encoding mutant proteins having increased angiogenic activity are disclosed. Expression vectors containing these sequences are introduced into host cells and direct the production of mutant angiogenic proteins with markedly increased angiogenic activity. Replacement of amino acids in a region at or corresponding to residues 8-22 ofangiogenin, with other amino acids, in particular, with amino acids corresponding to residues 7-21 of RNase, unexpectedly yields a mutant angiogenin/RNase hybrid protein with I 0-fold increased angiogenic