Effect of transmembrane potential on noradrenaline transport in chromaffin granules]

Imposing a transmembrane potential positive with respect to the medium on chromaffin granule ghosts increased the initial rate of the delta pH-induced uptake of noradrenaline, whereas imposing a negative potential decreased this rate. The increase of the uptake rate was proportional to the potential. The ATP-induced uptake of noradrenaline was also sensitive to the potential since imposing a transient negative potential onto the positive potential generated by the membrane ATPase induced a latency in this transport.     

Étude biochimique des poissons: 2. Variations semestrielles de la teneur en glycogène,en lipides totaux et en minéraux du tissu musculaire de la truite Arc-en-ciel (Salmo gairdnerii Rich)

Summary The variations of glycogen, lipids and ashes in muscular tissue of the Rainbow trout (Salmo gairdnerii Rich.) show that during sexual cycle there are 4 periods. Each period corresponds to a particular biological activity. The sexual activity cannot explain all the modifications of glycogen content.     

Unravelling the signal-transduction network in B lymphocytes

The Alliance for Cellular Signaling has chosen the mouse B lymphocyte as a model system to understand basic principles that govern cellular signalling. Progress to that end has focused initially on establishing a reproducible experimental cell system and characterizing essential signalling responses. Although unravelling this complex network will take years, findings revealed in the interim will prove immensely useful to the scientific community at large.     

Femtosecond X-ray protein nanocrystallography

X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded. It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been determined despite their importance in all living cells. Here we present a method for structure determination where single-crystal X-ray diffraction 'snapshots' are collected from a fully hydrated stream of nanocrystals using femtosecond pulses from a hard-X-ray free-electron laser, the Linac Coherent Light Source. We prove this concept with nanocrystals of photosystem I, one of the largest membrane protein complexes. More than 3,000,000 diffraction patterns were collected in this study, and a three-dimensional data set was assembled from individual photosystem I nanocrystals (～200?nm to 2?μm in size). We mitigate the problem of radiation damage in crystallography by using pulses briefer than the timescale of most damage processes. This offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage.