The sheepshead has two readily isolatable humoral immunoglobulins, a 16S tetrameric form and a 6S monomeric form. The 16S tetrameric form is composed of two subpopulations, one being a disulfide linked form (~700,000 daltons) and the other a noncovalently linked population of predominantly disulfide linked dimers (~350,000 daltons). The 6s immunoglobulin (~140,000 daltons) is composed of two noncovalently linked units (~70,000 daltons) each having one heavy and one light chain. The 6S immunoglobulin is antigenically deficient to the 16S immunoglobulin, this deficiency may be due to the heavy chain of the 6s protein lacking a~25,000 dalton segment present in the heavy chain of the 16S molecule.
Cutaneous mucus and bile also contain immunoglobulins. The mucus contains three proteins that can be considered immunoglobulins: a 6S form which is antigenically indistinguishable from the serum 6S immunoglobulin: a ~700,000 dalton form which does not have a "dimeric" subpopulation as observed with the serum 16S protein; and a dimeric form of ~350,000 daltons. The dimeric form may have a secretory piece since the reduced mucus dimeric protein shows an additional polypeptide chain at ~95,000 daltons. All of the cutaneous mucus high molecular weight immunoglobulins have heavy and light chains identical to the serum high molecular weight immunoglobulins (~70,000 and ~25,000 daltons).
Bile immunoglobulin is dimeric and composed of two noncovalently linked monomers of ~l60,000 daltons. The bile heavy chains are ~55,000 daltons; the light chains are ~25,000 daltons. The bile immunoglobulin does not appear to be a different class of protein from that of the serum or mucus immunoglobulins.
In vivo administration of radiolabeled 16S and 6S serum immunoglobulins indicates that the 6S protein is not a degradation product of the 16S form. The half lives of the 16S and 6s forms are both ~16 days.
Furthermore, the secretory immunoglobulins of the bile and mucus are not due to simple transudation or active transport of the predominant serum immunoglobulins. This result suggests that the secretory immunoglobulins of the sheepshead may be locally synthesized.
| Identifer | oai:union.ndltd.org:UTAHS/oai:digitalcommons.usu.edu:etd-8300 |
| Date | 01 May 1980 |
| Creators | Lobb, Craig J. |
| Publisher | DigitalCommons@USU |
| Source Sets | Utah State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | All Graduate Theses and Dissertations |
| Rights | Copyright for this work is held by the author. Transmission or reproduction of materials protected by copyright beyond that allowed by fair use requires the written permission of the copyright owners. Works not in the public domain cannot be commercially exploited without permission of the copyright owner. Responsibility for any use rests exclusively with the user. For more information contact digitalcommons@usu.edu. |
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