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In original essays, fourteen nationally known scholars examine the practical, philosophical, and epistemological implications of a variety of research traditions. Included are discussions of historical, theoretical, and feminist scholarship; case-study and ethnographic research; text and conversation analysis; and cognitive, experimental, and descriptive research. Issues that cross methodological boundaries, such as the nature of collaborative research and writing, methodological pluralism, the classification and coding of research data, and the politics of composition research, are also examined. Contributors reflect on their own research practices, and so reflect the current state of composition research itself.

Portfolios provide a mode of assessment that dovetails neatly with process theories about writing. As we have come to pay increasing attention to drafting and revision, and to the development of self-reflection and self-critical perceptions in the writer, many of us have increasingly come to value the idea of collecting students' work over time and evaluating the entire body of their writing. Grading students' work in pieces, product by product, or making significant judgments of students' writing based on one writing sample produced under timed circumstances, has come to seem a violation of the very things we teach about writing. For these reasons, talk about portfolios is everywhere. We hear of their use in school districts (Belanoff and Dixon; Camp and Levine; Murphy and Smith); in universities (Belanoff and Elbow; Elbow and Belanoff; Daiker et al.; Smit); in state assessments (Vermont Writing Assessment); in the British school system (General Certificate of Secondary Education English Literature Syllabus B), and elsewhere in the English speaking world. What we don't hear a great deal about is the process by which portfolios get proposed, designed, tested, and implemented. Since the rash of educational innovation in the late 1970s and early 1980s, educational theory has begun to view this process of implementation as a field in itself. Implementation studies examine the processes of innovative change and their meanings, often revealing the difficulties and complexities of attempts at systemic change (see Fullan; and for an earlier view, Miles). But we who do most of our work in English studies often focus our attention principally on our proposed designs and the intended outcomes, not on the all-important ways that the pro

In late nineteenth-century Hawaii, trading ships brought to the islands, among other things, an infestation of rats. As one way of dealing with the ensuing health problems, authorities decided to import mongooses, lithe, greybrown creatures which feed on small rodents. A shipment was therefore brought from India and set loose on the rat population of Hawaii. But things did not turn out as expected, for the mongoose proved to be a diurnal creature, a hunter by day, while the rat worked nights. The two animals thus lived side by side but very seldom met, and both populations flourished. Now Hawaii has a rat problem and a mongoose problem. Since 1984, I have been a co-author of the twice-yearly annotated bibliography of research for Research in the Teaching of English (RTE). In that time, I have observed a similar pattern occurring in composition studies. Researchers and theorists perceive a problem. A remedy is proposed-a new line of research, one of instruction, or more commonly a mixture of both. The remedy is implemented, only to reveal a new set of problems and concerns. Sometimes the research question may even be largely resolved, yet problems and concerns remain. For example, we have learned a great deal about how virtually every type of writer composes, from poets (Armstrong) to professors (Levi and Grasha), to pre-school children (Cox and Sulzby). But amidst the neat rows of results come new and even more beguiling questions: What good is knowledge of writers' processes without equally detailed knowledge of the contexts

Oligomycin-sensitive adenosine triphosphatase (ATPase) has been purified in large yields from yeast mitochondria by a procedure employing Sepharose 6B chromatography. The nature of the oligomycin binding site in this purified preparation has been studied by an affinity labeling technique in which oligomycin binding to the ATPase complex was followed by reduction of the complex with sodium [3H]borohydride. A major incorporation of label into protein with a molecular weight near 8000 was noted. This incorporation is dependent on the presence of oligomycin, is blocked by dicyclohexylcar-bodiimide, and is altered by mutations conferring oligomycin resistance to the ATPase. The evidence suggests that the low molecular weight proteolipid component of the ATPase complex is the site of oligomycin binding.

A group of oligomycin-resistant mutants of Saccharomyces cerevisiae have been selected. Most are cytoplasmically inherited and have altered ATPase sensitivity in isolated mitochondria. Two mutants, resistant to growth on oligomycin, are not resistant when ATPase is tested in isolated mitochondria. One of these mutants shows normal Mendelian inheritance while the other is cytoplasmic. Studies on the isolated soluble ATPase enzyme from wild type cells show that the solubilized enzyme is not inhibited by oligomycin but the reconstituted enzyme complex is sensitive. ATPases from oligomycin-resistant mutants can also be separated into their component parts and subsequently reconstituted. The reconstituted enzyme complex resembles the mitochondrial-bound enzyme in its resistance to oligomycin inhibition. Preparation of hybrid reconstituted ATPase complexes from mixed components of the mutant and wild type enzymes shows that the resistance is contributed by the membrane fraction of the mutant ATPase. Thus, the mitochondrial DNA has been shown to direct the synthesis of a membrane component influencing the activity of the mitochondrial ATPase.

Soybean (Glycine max [L.] Merrill, cv. Dare) suspension cultures grown in Gamborg B5 medium became discolored and the cells began aggregating after 1 week in culture, especially in the absence of 2,4-dichlorophenoxyacetic acid (2,4-D). The addition of either soluble polyvinylpyrrolidine (PVP) or bovine serum albumin (BSA) to cultures grown in Gamborg B5 medium with 2,4-D prevents discoloration and cell aggregation by adsorbing excess polyphenols from the cells. Transfer of the PVP-treated cultures to fresh medium without 2,4-D stimulated the recurrence of excess polyphenols. Cultures pretreated with BSA did not develop excess polyphenols when transferred to fresh 2,4-D-free medium. Addition of either PVP or BSA to cultures grown in the absence of 2,4-D was found to inhibit growth.

Human Factor VIII procoagulant protein (VIII:C) is a plasma protein that participates in the cascade of events leading to blood coagulation. It is absent or defective in patients with hemophilia A. In vivo Factor VIII:C associates with Von Willibrand factor and its multimers to form a high-molecular-weight particle that cna be dissociated into a lower-molecular-weight form in the presence of high concentrations of salt. We have been able to purify rapidly Factor VIII:C on a large scale by sequential high-performance size-exclusion chromatography (HPSEC) under conditions of first low salt and then high salt concentration. Reconstituted commercial Factor VIII:C concentrate was purified by chromatography on a preparative HPSEC column (Toyo Soda, 60 × 2.5 cm, 300ml) in 0.05 M imidazole buffer, (pH 7.0), containing 0.15 M sodium chloride. Factor VIII:C activity was eluted in the void volume in less than 20 min as a high-molecular-weight particle, well separated from low-molecular-weight contaminants. Purification was 20-fold, with a yield of 80%. Up to 4 g of Factor VIII concentrate could be purified at one time in this manner. This material was then concentrated and made 0.35 M in calcium chloride prior to re-chromatography on the same column in a buffer containing 0.30 M calcium chloride. Under these conditions, Factor VIII:C activity was eluted in the inner volume of the column at a position corresponding to a molecular weight of several hundred thousand in less than 1 h. It was well separated from both larger proteins and smaller peptide fragments. Analysis of the preparation with radiolabelled antibody to human Factor VIII:C antigen indicated that at least two molecular weight forms of Factor VIII:C were present.

Kinetin, and all other cytokinins tested, inhibited the conjugation of [(14)C]2,4-dichlorophenoxyacetic acid (2, 4-D) to amino acids when supplied simultaneously with the 2,4-D to cultured soybean cells. Upon transfer to hormone-free medium, the cytokinin-treated cells released more of their [(14)C]2,4-D than did the control cells. Initial exposure to low 2,4-D and high kinetin levels resulted in the greatest release of 2,4-D upon subsequent transfer. The observed alteration in 2,4-D metabolism did not seem to be correlated with growth rate. Appropriate treatment of soybean cells with kinetin resulted in 2,4-D metabolism that resembled the 2,4-D metabolism of embryogenic carrot cells. However, no new morphological structures were observed in these soybean cultures, indicating that other factors are related to the failure of soybean cells to regenerate in culture.

Many species of interferon have been identified and purified from human leukocytes, and genes for these interferons have been cloned in bacterial systems. However, it is still unclear as to how the expression of each of the different leukocyte interferons is regulated and how they function in the natural system. In preparation for a study of the in vivo role of individual leukocyte interferons we have developed a rapid and convenient high-performance liquid chromatographic method for purifying several species of human leukocyte interferon. Interferon produced by the induction of leukocytes (obtained from buffy coats of normal donors) with Sendai virus and partially purified by ethanol fractionation was further purified by size-exclusion high-performance liquid chromatography (on two Waters,I-125 columns) in 0.05 M sodium phosphate buffer, pH 6, containing 0.2 M sodium chloride. The flow-rate was 2 ml/min and interferon activity (antiviral) was eluted from the columns in less than 15 min in a single fraction well resolved from high-molecular-weight contaminants. This material was then purified by reversed-phase high-performance liquid chromatography on a wide-pore diphenyl column (Whatman Protesil 300) with a gradient system at pH 2.4, consisting of (A) 0.05 M KH2PO4—methoxyethanol (19:1) and (B) 1-propanol—methoxyethanol (19:1). Several peaks of interferon activity were distinguishable in this system. Analysis of the pooled peaks of interferon activity by SDS polyacrylamide gel electrophoresis confirmed the presence of more than one form of leukocyte interferon. The specific activity of the purified leukocyte interferers was ca. 108 units/mg protein.

Spectroscopic radial velocities for 83,072 stars in the Milky-Way southern hemisphere using the 6dF instrument at the AAO. Stellar parameters are published for a set of 39,833 stars belonging to the second and third years of observation. (1 data file).

Spectroscopic radial velocities for 83,072 stars in the Milky-Way southern hemisphere using the 6dF instrument at the AAO. Stellar parameters are published for a set of 39,833 stars belonging to the second and third years of observation.

A cooling device was developed to prevent the rapid breakdown of the quality of broken-out eggs displayed in open air educational settings. This device consists of a plastic container that holds a freezeable jell. Blue ice. Loose polystyrene is utilized for insulation. A petri dish set on the container lid will hold a broken-out egg. Egg quality can be held over a sufficient period of time for education or contest purposes.