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003 OCoLC;

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035 a| (Sirsi) o46972893;

035 a| (OCoLC)46972893;

049 a| EREE;

050 4 a| QL638.I3b| M33 2000;

100 1 a| Machon, Benjamin D.,e| author.?| UNAUTHORIZED;

245 10 a| Expression of the endoplasmic reticulum protein calnexin in the channel catfish, ictalurus punctatus /c| by Benjamin D. Machon.;

264 0 c| 2000.;

300 a| 51 leaves :b| illustrations (some color) ;c| 28 cm;

336 a| textb| txt2| rdacontent;

337 a| unmediatedb| n2| rdamedia;

338 a| volumeb| nc2| rdacarrier;

502 b| M.S.c| East Carolina Universityd| 2000;

500 a| Submitted to the faculty of the Department of Biology.;

500 a| Advisor: Thomas J. McConnell;

504 a| Includes bibliographical references (leaves 46-51).;

650 0 a| Channel catfish.=| ^A112918;

650 0 a| Endoplasmic reticulum.=| ^A359405;

650 7 a| Channel catfish.2| fast0| (OCoLC)fst00852101;

650 7 a| Endoplasmic reticulum.2| fast0| (OCoLC)fst00909799;

655 7 a| dissertations.2| aat0| (CStmoGRI)aatgf300028029;

655 7 a| Academic theses.2| fast0| (OCoLC)fst01726453;

655 7 a| Academic theses.2| lcgft;

655 7 a| Thèses et écrits académiques.2| rvmgf0| (CaQQLa)RVMGF-000001173;

700 1 a| McConnell, Thomas J.,e| degree supervisor.?| UNAUTHORIZED;

710 2 a| East Carolina University.b| Department of Biology.=| ^A637467;

856 41 z| Access via ScholarShipu| http://hdl.handle.net/10342/12562;

880 3 6| 520-00a| The molecular chaperone calnexin is a resident endoplasmic reticulum (ER) protein that functions in quality control by preventing immature, unassembled and misfolded glycoproteins from exiting the ER. Calnexin binds newly synthesized glycoproteins in the ER containing monoglucosylated (Glc1Man9GlcNac2) N-linked glycans, generated by the concerted actions of the glucose trimming enzymes, glueosidase I, glucosidase II and and the reglucosylation enzyme UDP-glucose glycoprotein glucosyltransferase. Calnexin has been found to associate with many glycoproteins including class II MHC α and β and invariant chain proteins. However the majority of information about MHC class II maturation has been discovered using mammalian cell types. Here the channel catfish, Ictalurus punctatus, was used as a model system to analyze chaperone function in a teleost. As an important first step towards understanding quality control of MHC class II assembly in teleosts, a series of experiments was performed to determine if calnexin is present and functional in Ictalurus. Immunopřcipitation and Western Blotting experiments have determined the presence of calnexin in an Ictalurus punctatus B cell line. It was also determined that anti-invariant chain antibodies assayed reacted specifically with murine invariant chain molecules, but did not crossreact with a putative catfish invariant chain. Using an anti- catfish MHC class II β antibody it also was ascertained that newly synthesized class II molecules can also be precipitated with this reagent and the association of MHC class II β and calnexin might be weak in the catfish when compared to mammals.;

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Expression of the endoplasmic reticulum protein calnexin in the channel catfish, ictalurus punctatus / by Benjamin D. Machon.

Author/creator	Machon, Benjamin D. author.
Other author	McConnell, Thomas J., degree supervisor.
Other author	East Carolina University. Department of Biology.
Format	Theses and dissertations
Production	2000.
Description	51 leaves : illustrations (some color) ; 28 cm
Supplemental Content	Access via ScholarShip
Subjects	Channel catfish. Endoplasmic reticulum.

General note	Submitted to the faculty of the Department of Biology.
General note	Advisor: Thomas J. McConnell
Dissertation note	M.S. East Carolina University 2000
Bibliography note	Includes bibliographical references (leaves 46-51).
Genre/form	dissertations.
Genre/form	Academic theses.
Genre/form	Academic theses.
Genre/form	Thèses et écrits académiques.

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Expression of the endoplasmic reticulum protein calnexin in the channel catfish, ictalurus punctatus / by Benjamin D. Machon.

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