Brandon/Hill selected list of print books and journals in allied health*

This list of 424 books and 77 journals is intended as a selection guide for print literature to be used in a library supporting allied health educational programs or allied health personnel in either an academic or health care setting. Because of the impossibility of covering the large number and wide variety of allied health professions and occupations, the recommended publications are focused primarily on the educational programs listed and recognized by the American Medical Association and other accrediting bodies. Books and journals are categorized by subject; the book list is followed by an author/editor index, and the subject list of journals by an alphabetical title listing. Items suggested for initial purchase (167 books and 31 journals) are indicated by asterisks. To purchase the entire collection of books and journals (2000 subscriptions) would require an expenditure of about $31,970. The cost of only the asterisked items totals $12,515.

Brandon/Hill selected list of print books and journals for the small medical library*

After thirty-six years of biennial updates, the authors take great pride in being able to publish the nineteenth version (2001) of the “Brandon/Hill Selected List of Print Books and Journals for the Small Medical Library.” This list of 630 books and 143 journals is intended as a selection guide for health sciences libraries or similar facilities. It can also function as a core collection for a library consortium. Books and journals are categorized by subject; the book list is followed by an author/editor index, and the subject list of journals, by an alphabetical title listing. Due to continuing requests from librarians, a “minimal core list” consisting of 81 titles has been pulled out from the 217 asterisked (*) initial-purchase books and marked with daggers (†*) before the asterisks. To purchase the entire collection of 630 books and to pay for 143 2001 journal subscriptions would require $124,000. The cost of only the asterisked items, books and journals, totals $55,000. The “minimal core list” book collection costs approximately $14,300.

Chromophore-assisted light inactivation and self-organization of microtubules and motors

Chromophore-assisted light inactivation (CALI) offers the only method capable of modulating specific protein activities in localized regions and at particular times. Here, we generalize CALI so that it can be applied to a wider range of tasks. Specifically, we show that CALI can work with a genetically inserted epitope tag; we investigate the effectiveness of alternative dyes, especially fluorescein, comparing them with the standard CALI dye, malachite green; and we study the relative efficiencies of pulsed and continuous-wave illumination. We then use fluorescein-labeled hemagglutinin antibody fragments, together with relatively low-power continuous-wave illumination to examine the effectiveness of CALI targeted to kinesin. We show that CALI can destroy kinesin activity in at least two ways: it can either result in the apparent loss of motor activity, or it can cause irreversible attachment of the kinesin enzyme to its microtubule substrate. Finally, we apply this implementation of CALI to an in vitro system of motor proteins and microtubules that is capable of self-organized aster formation. In this system, CALI can effectively perturb local structure formation by blocking or reducing the degree of aster formation in chosen regions of the sample, without influencing structure formation elsewhere.

Kinetic coupling between electron and proton transfer in cytochrome c oxidase: simultaneous measurements of conductance and absorbance changes.

Bovine heart cytochrome c oxidase is an electron-current driven proton pump. To investigate the mechanism by which this pump operates it is important to study individual electron- and proton-transfer reactions in the enzyme, and key reactions in which they are kinetically and thermodynamically coupled. In this work, we have simultaneously measured absorbance changes associated with electron-transfer reactions and conductance changes associated with protonation reactions following pulsed illumination of the photolabile complex of partly reduced bovine cytochrome c oxidase and carbon monoxide. Following CO dissociation, several kinetic phases in the absorbance changes were observed with time constants ranging from approximately 3 microseconds to several milliseconds, reflecting internal electron-transfer reactions within the enzyme. The data show that the rate of one of these electron-transfer reactions, from cytochrome a3 to a on a millisecond time scale, is controlled by a proton-transfer reaction. These results are discussed in terms of a model in which cytochrome a3 interacts electrostatically with a protonatable group, L, in the vicinity of the binuclear center, in equilibrium with the bulk through a proton-conducting pathway, which determines the rate of proton transfer (and indirectly also of electron transfer). The interaction energy of cytochrome a3 with L was determined independently from the pH dependence of the extent of the millisecond-electron transfer and the number of protons released, as determined from the conductance measurements. The magnitude of the interaction energy, 70 meV (1 eV = 1.602 x 10(-19) J), is consistent with a distance of 5-10 A between cytochrome a3 and L. Based on the recently determined high-resolution x-ray structures of bovine and a bacterial cytochrome c oxidase, possible candidates for L and a physiological role for L are discussed.