Properdin is a serum glycoprotein that upregulates the alternative pathway of complement by stabilizing the C3bBb complex. It also binds sulphated glycoconjugates, such as sulphatide, in vitro. Properdin is composed of cyclic dimers, trimers and tetramers of a 53 kDa monomeric subunit. The monomer contains an N-terminal region of no known homology and six thrombospondin type 1 repeats (TSRs) of approximately sixty amino acids. The sixth TSR of properdin contains an insertion of approximately 30 amino acids which corresponds to the position of an intron in the human properdin gene. In order to identify the regions of properdin important for function, human properdin, and mutant forms each lacking a single TSR, were expressed in Chinese Hamster Ovary cells. In addition, limited tryptic digestion yielded "nicked" properdin by the cleavage of one peptide bond in TSR5. The structural and functional properties of the normal and altered forms of properdin were investigated. Wild type recombinant properdin is similar to properdin purified from plasma in size, immunoreactivity, N-terminal sequence, possession of N-linked sugar, oligomerization (as determined by electron microscopy and gel exclusion chromatography), and functional activity in an alternative pathway haemolytic assay, and in C3b and sulphatide binding assays. Properdin "nicked" in TSR5 is unable to bind C3b, while retaining its overall structure and its ability to bind sulphatide. The removal of TSRS prevents C3b and sulphatide binding. Properdin lacking TSR4 is unable to stabilize the C3bBb complex, but is able to bind C3b and sulphatide, and shows the presence of monomers and dimers in the electron microscope. Properdin without TSR3 is able to stabilize the C3bBb complex, to bind CSb and sulphatide, and forms dimers, trimers and tetramers. Properdin lacking TSR6 is unable to form oligomers. The N-linked carbohydrate of properdin is not required for oligomerization or stabilization of the C3bBb complex. Monoclonal antibodies which bind to the N-terminal region, TSR1, or TSR2 are able to inhibit properdin binding to CSb. A monoclonal antibody which binds TSR4 is able to inhibit properdin binding to sulphatide, but not to CSb. The results confirm that TSRs are folded as independent units. The N-terminal end and TSR5 of properdin are implicated in CSb binding. The vertices of properdin oligomers may be important for interaction with CSb. TSR4 may also be involved in stabilization of the C3bBb complex. The sulphatide binding site is distinct from the CSb binding site, but TSR5, which contains many basic residues, may be important for both activities.

Typescript. / Thesis (Ph. D.)--University of Hawaii, 1966. / Bibliography: leaves 88-91. / xii, 91 l illus., tables

Thesis (M. Sc.)--University of Canterbury, 2006. / Typescript (photocopy). Includes bibliographical references (leaves 85-95). Also available via the World Wide Web.

Thesis (M.S.)--Wisconsin. / Includes bibliographical references (leaves 45-60).

Academisch proefschrift - Utrecht. / Summary in Dutch and English. Cover title: Electrophorese en serumvlokkingsreacties.

Thesis (Ph. D.)--University of Wisconsin--Madison, 1968. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.

Thesis (M.S.)--Oregon State University, 2007. / Printout. Includes bibliographical references (leaves 68-77). Also available on the World Wide Web.

Thesis (Ph.D.)--University of Nebraska-Lincoln, 2008. / Title from title screen (site viewed Feb. 17, 2009). PDF text: ix, 137 p. : ill. (some col.) ; 2 Mb. UMI publication number: AAT 3325856. Includes bibliographical references. Also available in microfilm and microfiche formats.

No description available.

After standardizing a starch-gel electrophoretic technique, variations in the serum proteins of the genus Odocoileus due to the condition of the sample and the condition of the animal were studied. Significant changes in the serum sample were brought about by hemolysis, cloudiness, and decomposition. Cold storage for two years of adult deer serum, the addition of a bacteriostat to the sample, and the use of a muscle relaxant to procure samples from captive deer produced no significant changes in either the mobility or the percent composition of the protein fractions. A large individual variation was found in both the mobility and the percent composition of the protein fractions. The percent composition of the protein fractions was affected by sex, age, and season. The mobility of the protein fractions was affected by sex, but not by age or season. Captive deer at the University of British Columbia exhibited an additional negatively migrating protein fraction when compared to their wild counterparts. Comparisons of the mobilities in three groups of adult females of the genus Odocoileus indicate greater intra-subspecific differences than inter-specific differences. The technique of starch-gel electrophoresis, therefore, may be useful in individual and herd recognition but it is not useful in the recognition of subspecies or species of deer of the genus Odocoileus. / Science, Faculty of / Zoology, Department of / Graduate