PubMed Health⌕ Search

Biomedical subjects

F Alba

Publications and source records attributed to F Alba.

79 records · Page 5Linked to original sources
PubMedDate not supplied

[Interhemispherical study of the activities of aminopeptidases, lactate dehydrogenase and glutamate-oxaloacetate transaminase in the rat brain].

Aminopeptidase activity has been assayed from both soluble and membrane bound fractions in eleven regions of the left and right hemispheres of the rat brain, using L-leucine-2-naphthylamide as substrate. Two other metabolic enzymes, lactate dehydrogenase and glutamate-oxalacetate aminotransferase activities were simultaneously determined in the same areas. When individual zones of the left hemisphere were compared with its corresponding right zones, soluble aminopeptidase activities were significantly higher in left frontal cortex and left hypothalamus than in right frontal cortex and right hypothalamus, respectively. No other significant differences were found neither in the remaining areas nor for the other enzymatic activities between both brain hemispheres.

Aminopeptidases↗
PubMedDate not supplied

[Demographic and economic development in contemporary Mexico].

This paper briefly reviews the main features of the recent Mexican experience in demographic and economic development matters. It assesses the development pattern that prevailed between 1940 and 1970 and the ways and policies that were instrumental in accommodating the rapid population growth of the period. The author considers that by 1970 the relatively acceptable demo-economic system in place since 1940 entered a period of emerging tensions, and examines the responses to those difficulties, among them the change in population policy. It closes with a brief review of the tasks ahead considering future demographic and economic tendencies in Mexico.

Demography↗
PubMedDate not supplied

[A fluorimetric method for the determination of brain aminopeptidases].

A fluorometric method adapted to the determination of brain aminopeptidase activities has been developed in our laboratory. This method is based in the fluorescence produced by 2-naphthylamine when it is released from aminoacyl-2-naphthylamides under the hydrolytic action of these enzymes. Values of enzymatic activities and kinetic constants are similar to those previously described in the literature.

Aminopeptidases↗