Mean velocity of optically detected intraaxonal particles measured by a cross-correlation method.

A method which uses by the cross correlation of optical signals is described for the determination of the mean velocity of somatopetally moving particles within nerve fibers. The method was validated by simulation experiments and by comparing the results with those obtained by averaging collections of velocities of individual particles. The significant contribution of the method is that it allows objective and rapid serial evaluation of mean particle velocity within individual nerve fibers with good accuracy and precision. A series of results from normal myelinated nerve fibers from Xenopus laevis is presented. Considerable variation (up to 50%) in mean velocity was found between individual nerve fibers. The mean of all determinations indicates that the mean velocity of somatopetally moving particles in axons with diameters greater than 10mum is in the region of 1.14 mum/s at a temperature of 22-24 degrees C. The findings are compared with small collection of such determinations which have been reported in the literature.     

Prolactin binding to dissociated cells from rat mammary tumors and mammary gland.

Prolactin binding activity was studied in suspensions of cells which had been enzymatically dissociated from R3230AC mammary tumors, 7,12-dimethylbenz(a)anthracene (DMBA)-induced mammary tumors and lactating rat mammary glands. Prolactin bound specifically with high affinity (apparent binding affinity = 4.0 X 10(9) M-1) to R3230AC tumor cells. Hormone binding at room temperature was proportional to cell number and increased with time of incubation up to 120-180 min. Prolactin binding to R3230AC tumor cells from diabetic animals was reduced by about 50%. Specific prolactin binding activity was also demonstrated in preparations of cells from DMBA-induced tumors and lactating mammary gland. The levels of hormone binding in both dissociated cells and subcellular particles prepared from these tissues varied as follows: DMBA-induced tumors > lactating mammary gland > R3230AC mammary adenocarcinoma.     

Phosphorylation on basic amino acids in myelin basic protein.

Isolated rat brain myelin when incubated with γ³²P labelled ATP yields proteins bearing acid labile, base stable phosphoryl groups. Phosphorylated myelin basic protein can be isolated and degraded with trypsin and pronase to yield principally phosphoarginine and phosphohistidine. Only a very small amount of phosphorerine survives the base treatment used in the isolation procedure.