Molecular-basis For The Temperature-dependent Insolubility Of Cryoglobulins .10. The Amino-acid-sequence Of The Heavy-chain Variable Region Of Mce
Immunology
Gerberjenson B; Kazin A; Kehoe J M; Scheffel C; Erickson B; Litman G W
Journal of Immunology
1981
1981
Journal Article or Conference Abstract Publication
n/a
Mouse Alpha-macroglobulin - Structure, Function And A Molecular-model
Biochemistry & Molecular Biology; Cell Biology; Life Sciences & Biomedicine - Other; Topics
Hudson N W; Kehoe J M; Koo P H
Biochemical Journal
1987
1987-12
Journal Article or Conference Abstract Publication
<a href="http://doi.org/10.1042/bj2480837" target="_blank" rel="noreferrer noopener">10.1042/bj2480837</a>
Structural Comparison Of A Murine Alpha-2-antiproteinase With Human Alpha-2-macroglobulin
Life Sciences & Biomedicine - Other Topics
Hudson N; Koo P H; Kehoe J M
Federation Proceedings
1980
1980
Journal Article or Conference Abstract Publication
n/a
Immunoglobulin Structure And Function - Genetic-control Of Antibody Diversity
Veterinary Sciences
Kehoe J M; Seide R K
Journal of the American Veterinary Medical Association
1982
1982
Journal Article or Conference Abstract Publication
n/a
The structure of immunoglobulin variable regions in the horned shark,Heterodontus francisci.
The heavy and light chains of pooled antibodies of the hybodont shark,Heterodontus francisci (horned shark), were subjected to amino acid sequence analysis. Yield determinations showed that more than 90% of the available polypeptides in the respective pools were sequenced. The heavy chains were homogeneous in the initial framework segment and showed a sequence homology of approximately 70% with the corresponding region of the more recently evolved nurse shark and a 45% homology with a human myeloma heavy chain. The light chains were less homogeneous and not identifiable as either kappa or lambda chains as known in higher species. The first half-cystine characteristics of the variable domain intrachain disulfide bridge of immunoglobulins was present in the same position (22 for heavy chains; 23 for light chains) in the horned shark as in mammalian species. The sequence analysis also suggested the presence of a hypervariable region in the horned shark light chains. The combined data imply that the antigen-binding function of immunoglobulins is mediated in much the same manner in this primitive shark as in more recently evolved species, including mammals.
Kehoe J M; Sharon J; Gerber-Jenson B; Litman G W
Immunogenetics
1978
1978-12
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
<a href="http://doi.org/10.1007/BF01843985" target="_blank" rel="noreferrer noopener">10.1007/BF01843985</a>
INHIBITION OF THE CLASSICAL COMPLEMENT PATHWAY BY SYNTHETIC PEPTIDES FROM THE SECOND CONSTANT DOMAIN OF THE HEAVY-CHAIN OF HUMAN IMMUNOGLOBULIN-G
Biochemistry & Molecular Biology
Prystowsky M B; Kehoe J M; Erickson B W
Biochemistry
1981
1981
Journal Article
<a href="http://doi.org/10.1021/bi00525a010" target="_blank" rel="noreferrer noopener">10.1021/bi00525a010</a>
Characterization of a homogeneous paraprotein from a horse with spontaneous multiple myeloma syndrome.
Male; Animals; Horse Diseases/*immunology; Horses/immunology; Immunoglobulin Light Chains/*isolation & purification; Multiple Myeloma/immunology/*veterinary; Myeloma Proteins/*isolation & purification
A novel myeloma paraprotein has been isolated from a horse with a lymphoid tumor. The protein was a euglobulin and consequently was readily isolated from serum in pure form and high yield by simple dilution in distilled water. The purified intact protein had a molecular weight of 150,000 and was composed of heavy and light chains, both of which had blocked amino-termini and were thus not susceptible to amino-terminal sequence analysis. The amino acid compositions of these respective chains corresponded to those of comparable chains from immunoglobulins of other species. Peptide maps of paraprotein light chains prepared by high pressure liquid chromatography corresponded in part to those of normal pooled equine light chains. The identification of this paraprotein as an equine AI (aggregating immunoglobulin) protein was confirmed by serological analysis using a specific antiserum. The relationship of this particular protein to other members of the immunoglobulin family was further demonstrated by the production of an anti-idiotypic antiserum individually specific for this molecule.
Seide R K; Jacobs R M; Dobblestein T N; Kehoe J M
Veterinary immunology and immunopathology
1987
1987-12
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
<a href="http://doi.org/10.1016/0165-2427(87)90128-0" target="_blank" rel="noreferrer noopener">10.1016/0165-2427(87)90128-0</a>
ISOLATION AND CHARACTERIZATION OF A HOMOGENEOUS EUGLOBULIN FROM THE SERUM OF A HORSE WITH A SPONTANEOUS MULTIPLE-MYELOMA SYNDROME
Life Sciences & Biomedicine - Other Topics
Seide R K; Jacobs R M; Kehoe J M
Federation Proceedings
1982
1982
Journal Article
n/a
THE GENETIC-CONTROL OF ANTIBODY-FORMATION
Immunology; Veterinary Sciences
Seide R K; Kehoe J M
Veterinary Immunology and Immunopathology
1983
1983
Journal Article
<a href="http://doi.org/10.1016/0165-2427(83)90055-7" target="_blank" rel="noreferrer noopener">10.1016/0165-2427(83)90055-7</a>
STRUCTURAL-ANALYSIS OF HUMAN LYSOSOMAL GLUCOCEREBROSIDASE BY HPLC
Genetics & Heredity
Seide R; Hall J; Kehoe J M
American Journal of Human Genetics
1983
1983
Journal Article
n/a