Thesis (Ph. D.)--University of Oulu, 1986. / Includes bibliographical references (p. [44]-60).

Thesis--Wisconsin. / Vita. Includes bibliographical references (leaves 162-175).

No description available.

This document only includes an excerpt of the corresponding thesis or dissertation. To request a digital scan of the full text, please contact the Ruth Lilly Medical Library's Interlibrary Loan Department (rlmlill@iu.edu).

This thesis describes an immunochemical and immunocytochemical study of the bovine brain S-lOOb protein. The two major forms of the S-100 isoproteins (S-lOOa and S-lOOb) were purified to apparent homogeneity from bovine brain. A polyclonal rabbit antiserum to the S-lOOb protein was prepared. The antiserum was characterized by solid phase immunochemical methods. The S-lOOb derived antiserum displayed a high degree of specificity for S-lOOb, but also crossreacted with the purified S-lOOa protein. The characteristics of the immunochemical reactivity of the antiserum towards these two isoproteins suggests the antiserum has specificity for the 6-subunit of the S-100 proteins. An immunohistochemical analysis of the cellular localization of S-lOOb immunoreactivity was undertaken. In the adult rat brain only the astrocytes were S-lOOb immunoreactive. This conclusion is supported by the morphological characteristics of the immunolabelled cells, as well as the observed co-localization of the immunoreactivities for S-lOOb and the Glial Fibrillary Acidic protein (GFAP), the major protein of the astrocyte intermediate filaments. These two antigens were always found to coexist. The immunolabelling of rat brain astrocytes by the S-lOOb derived antiserum stained the entire cell, yielding more complete morphological detail than is possible with the GFAP immunohistochemistry, which only labels the filamentous glial processes. It is concluded that S-lOOb immunohistochemistry could be of general utility in the investigation of astrocyte morphology. The present results also determine that the as yet unknown biological function(s) of the S-100 proteins must be related to a property of astrocytes. / Medicine, Faculty of / Graduate

Thesis (Ph. D.)--University of Texas at Austin, 2002. / Vita. Includes bibliographical references. Available also from UMI Company.

Not available / text

Thesis (Ph. D.)--Georgia State University, 2007. / Vincent Rehder, committee chair; Sarah Pallas, Walter William Walthall, committee members. Electronic text (248 p. : ill. (some col.)) : digital, PDF file. Description based on contents viewed Jan. 28, 2008; title from file title page. Includes bibliographical references (p. 218-248).

Methylmalonyl CoA mutase has been purified over 2300-fold from bovine brain using fractional precipitation, ion exchange resins, and gel filtration procedures. The crude extract had an equal mixture of mutase in the halo- and apoenzyme form. After the final purification step the ratio had changed to 86% holo-enzyme and 14% apoenzyme. The mutase enzyme had a pH optimum of 7. 0 in Tris-HCI buffer. The Km values for L-methylmalonyl CoA and succinyl CoA were 7.7 x 10^-4 M and 1.8 x 10^-4 M respectively. The equiIibrium constant in the direction of succinyl CoA formation was 19. Inhibition with N-ethylmalei-mide was noncompetitive with a K_i of 2.4 x 10^-3 M. The activity level of mutase in the brain was found to be about 5% of that found in liver.

This document only includes an excerpt of the corresponding thesis or dissertation. To request a digital scan of the full text, please contact the Ruth Lilly Medical Library's Interlibrary Loan Department (rlmlill@iu.edu).