Electron flow at the polarized mercury-water interface in the presence of membrane fragments rich in Na+−K+-Activated ATPase

Summary Measurements of interfacial electron flow indicate that membrane fragments rich in Na⁺–K⁺-ATPase are capable of absorbing and releasing electrons in the form of random currents at an electrode surface. The electron transporting system, which functions in the presence or absence of substrate and activating ions, may be part of or in contact with the enzyme system, but it is not related to the ATPase activity. The observed electron transport at an electrode surface resembles physiological electron transport processes in being reversible, in extending over the same range of potential, and in being affected by some of the chemicals that interfere with electron transport and oxidative phosphorylation in mitochondria. Our experiments do not provide sufficient evidence to identify the substances that are responsible for the random currents, but the results suggest that the electro-active substances are similar to those which are involved in the reactions at the second phosphorylation site in mitochondria. Experiments with this technique provide a new approach to the study of the mechanism of biological electron transport processes and their possible relation to ATP synthesis and hydrolysis.Supported by U.S. Public Health Service Research Career Development Award K3-GM-8158.     

Genetic Regulation of Ribonucleoside and Deoxyribonucleoside Catabolism in Salmonella typhimurium

Four enzymes involved in ribonucleoside and deoxyribonucleoside catabolism (deoxyribose-5-P aldolase, thymidine phosphorylase, phosphodeoxyribomutase, and purine nucleoside phosphorylase) are coded for by four closely linked structural genes on the Salmonella chromosome. The genetic order of these genes is (deoC-deoA-deoB-deoD)-serB-thr. Studies on polarity mutants and induction patterns indicate that the deoB and deoD genes may constitute a single operon and that the deoC and deoA genes may constitute a second closely linked operon.     

Reproductive response of a tropical mammal, the musk shrew (Suncus murinus), to photoperiod

Musk shrews (Suncus murinus) were maintained for 8 weeks in long (16 h light:8 h darkness) or short (8 h light:16 h darkness) daylengths. Males housed in short daylength had significantly lighter androgen-dependent sex accessory organs than did males kept in long daylengths. This same trend was noted in male sexual behaviour. However, the weights of the testes and epididymides and sperm numbers did not differ. Females housed in short daylengths had significantly lighter cervices and were less likely to demonstrate sex behaviour than animals kept in under long daylengths. Ovarian and uterine weights did not differ. These results suggest that the ability to respond to photoperiod can exist in tropical mammals, even if it is not used as a cue to time seasonal breeding.     

Size and charge heterogeneity of murine IgG-binding factors (IgG-BF)

Size and charge of murine IgG-binding factors (IgG-BF) were determined. Four different sources were used to produce the factors: a) cells of a T cell hybrid (T2D4) constitutively secreting IgG-BF upon incubation in serum-free medium, b) T2D4 cells incubated with mouse monoclonal IgG1 antibody in order to induce in vitro the production of isotype-specific IgG1-BF, c) T2D4 cells induced in vivo by passage as ascites in nude mice and incubated in serum-free medium, and d) in vivo alloantigen-activated T cells (ATC) incubated in serum-free medium. IgG-BF were affinity purified on Sepharose beads coated with rabbit or mouse IgG and identified by their biologic activities, i.e., inhibition of in vitro secondary IgG antibody production to SRBC and inhibition of rosette formation between Fc gamma receptor-positive spleen cells and rabbit IgG-sensitized erythrocytes. IgG-BF produced by either of these cell sources was found to be heterogeneous in both size and charge. In each case, IgG-BF activities were recovered in three fractions of apparent Mr-74,000 to 78,000, 35,000 to 40,000, and 19,000 to 23,000-and in four fractions of pI-4.7 (or 5.3, depending on experimental conditions), 6.5, 7.7, and 8.4. Moreover, IgG-BF translated in vitro from T2D4 poly A RNA by using rabbit reticulocyte lysate exhibited the same heterogeneity. Thus, IgG-BF contain different proteins exerting similar biologic activities.