Lake Region Healthcare Clinic Services 111 W Vernon Ave, Fergus Falls, MN 56537 2187392221 (phone), 2187396799 (fax)
Education:
Medical School University of North Dakota College of Medicine Graduated: 1994
Procedures:
Colposcopy Tubal Surgery Vaginal Repair Amniocentesis Cesarean Section (C-Section) D & C Dilation and Curettage Electrocardiogram (EKG or ECG) Hysterectomy Myomectomy Oophorectomy Ovarian Surgery Skin Tags Removal Vaccine Administration Vaginal Delivery
Conditions:
Abnormal Vaginal Bleeding Breast Disorders Candidiasis of Vulva and Vagina Complicating Pregnancy or Childbirth Conditions of Pregnancy and Delivery
Languages:
English Spanish
Description:
Dr. Norgard graduated from the University of North Dakota College of Medicine in 1994. He works in Fergus Falls, MN and specializes in Obstetrics & Gynecology. Dr. Norgard is affiliated with Lake Region Healthcare.
Center For Cancer & Blood Disorders 202 E Dr Hicks Blvd STE 3, Florence, AL 35630 2567600422 (phone), 2567600332 (fax)
Education:
Medical School University of Wisconsin Medical School Graduated: 1969
Languages:
English
Description:
Dr. Norgard graduated from the University of Wisconsin Medical School in 1969. He works in Florence, AL and specializes in Medical Oncology. Dr. Norgard is affiliated with Eliza Coffee Memorial Hospital, Helen Keller Hospital and Shoals Hospital.
John R. Kettman - Carrollton TX Michael V. Norgard - Plano TX
Assignee:
Board of Regents, The University of Texas - Austin TX
International Classification:
G01N 5300 G01N 33511 G01N 3353
US Classification:
435 7
Abstract:
Murine anti-Treponema pallidum monoclonal antibodies were employed in the detection of low numbers of pathogenic treponemes. Monoclonal antibodies were used as a primary antibody source in a solid-phase immunoblot assay system. All monoclonal antibodies assayed were capable of detecting ca. 1. times. 10. sup. 3 to 2. 5. times. 10. sup. 3 treponemes. Of 13 monoclonal antibodies examined, 3 were able to detect 10. sup. 3 virulent treponemes, and 1 of these antibodies was able to reveal the presence of as few as 500 organisms. Western blot analyses showed that all anti-T. pallidum monoclonal antibodies exhibiting high sensitivities for the detection of T. pallidum cells were directed against an abundant, 47,000-48,000 dalton surface-exposed antigen of the organism. With two possible exceptions, the monoclonal antibodies tested reacted specifically with T. pallidum, either purified or found within a high-contaminating tissue background, and not with Treponema phagedenis biotype Reiter, Haemophilus ducreyi, Neisseria gonorrhoeae, herpes simplex virus type 2, or normal rabbit testicular tissue.
Board of Regents, The University of Texas System - Austin TX
International Classification:
C12N 1531
US Classification:
536 237
Abstract:
The present disclosure provides the complete primary amino acid, and underlying DNA, sequence for the 47-kilodalton surface immunogen of Treponema pallidum, subsp. pallidum. The sequence was obtained by using a combined strategy of DNA sequencing of the cloned gene as well as confirmatory N-terminal amino acid sequencing of the native antigen. An open reading frame corresponding to the 47-kDa antigen was comprised of 367 amino acid codohs, which gave rise to a calculated molecular weight for the corresponding antigen of about 40,701. Also disclosed are methods for preparing variant and mutant molecules having biologically similar attributes, as well as methods for preparing particular antigenic/immunogenic subportions of the 47-kDa protein. In particular aspects, antigenic/immunogenic subportions are identified by hydrophilicity analysis of the protein sequence. The 47-kDa antigen and antigenic subportions of the present invention can be used both as antigens in the detection of clinical materials having anti-47-kDa antibodies therein, as well as in the preparation of vaccines for use in connection with promoting an immune state in vaccinated individuals.
Hybrid Cell Lines Producing Monoclonal Antibodies Directed Against Treponema
John R. Kettman - Carrollton TX Michael V. Norgard - Plano TX
Assignee:
The Board of Regents, The University of Texas System - Austin TX
International Classification:
C12N 500 C12N 1500 C07G 700
US Classification:
435240
Abstract:
Continuous hybrid cell lines for producing monoclonal antibodies directed against antigens of Treponema pallidum have been developed. The hybrid cell lines were established by fusing differentiated lymphoid cells primed with antigens of Treponema pallidum with hybridoma cells. The resulting fused cells were cloned, isolated, cultured and characterized as to antibody specificity against antigenic determinants of Treponema pallidum.
Cloning And Expression Of The 47-Kilodalton Antigen Of Treponema Pallidum
Board of Regents, The University of Texas System - Austin TX
International Classification:
C12N 120 C12N 1500 C12R 1185
US Classification:
43525233
Abstract:
Monoclonal antibodies directed against the 47 kDa major outer membrane surface immunogen of virulent Treponema pallidum were used to select E. coli recombinant clones expressing the 47 kDa immunogen. The phenotype of the clones was dependent on the presence of recombinant plasmid in the host cell. Southern hybridization revealed that The United States government may have rights in the substance of this patent because of developmental work supported by the U. S. Department of Health and Human Services in the form of research grants 1-R01-AI-16692 and 1-R01-AI-17366 from NIH-NIAID.
Board of Regents, The University of Texas System - Austin TX
International Classification:
C07K 1420 C12N 1531
US Classification:
530403
Abstract:
The present disclosure provides the complete primary amino acid, and underlying DNA, sequence for the 47-kilodalton membrane immunogen of Treponema pallidum, subsp. pallidum. The sequence was obtained by using a combined strategy of DNA sequencing of the cloned gene as well as confirmatory N-terminal amino acid sequencing of the native antigen. An open reading frame corresponding to the 47-kDa antigen was comprised of 434 amino acid codons. This open reading frame contained a typical 19 amino acid hydrophobic leader peptide flanked by a consensus sequence of Val-Val-Gly-Cys for signal peptidase II, the lipoprotein-specific signal peptidase of prokaryotes. The molecular weight of the mature molecule, excluding modification, is 45,756. Also disclosed are methods for preparing variant and mutant molecules having biologically similar attributes, as well as methods for preparing particular antigenic/immunogenic subportions of the 47-kDa protein. In particular aspects, antigenic/immunogenic subportions are identified by hydrophilicity analysis of the protein sequence.