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1.
Article in Portuguese | LILACS | ID: lil-592560

ABSTRACT

During the course of a study on the behaviour, of Stomoxys calcitrans a research on the feeding habits of this fly was carried out. A total of 27l4 flies were caught in three poultry ranches from Araucária, Paraná. The source of the flie's sucked blood has been established by precipitin test. . The results showed that although almost all the flies usually feed mammal blood, some of them gave positive precipitin test for birds blood. Although all flies were caught on poultry ranches, none had feed on chickens but 2,7 percent of the total had feed on ducks, 0.7 percent on geese and 0.37 percent on turkeys.

2.
Arq. biol. tecnol ; 32(3): 575-87, ago. 1989. ilus, tab
Article in English | LILACS | ID: lil-74261

ABSTRACT

An inducible L-fucose dehydrogenase from the yeast-like fungus Pullularia pullulans was purified and studied. The enzyme catalyses the oxidation of L-fucose to L-fuconic acid possibly throught its unstable L-funcono-lactone. the enzyme was purified to hemogeneity by a sequence of protamine sulfate treatment, ammonium sulfate fractionation, gel filtration on Sephadex G-100, and DEAE-cellulose chromatography. This sequence resulted in an 87 fold purification. The apparent molecular weight determined by gel filtration and SDS polyacrilamide gel electrophoresis was 40 000. the dehydrogenase was NAD-especific and showed a high sugar substrate specificity. Of several D-and L-aldoses tested only L-fucose, L-galactose and-arabinose served as substrates. The maximum velocity for the reaction was at 33- and pH 10.5. Under these conditions, the Km values, and D-arabinose, respectively. The enzyme was strongly inhibited by thiol reagents, heavy metal ions, and was not particularly stable. At 4- it rapidly los activity, but remained active for two months when maintained at -20-. The enzyme has been used to quantativate L-fucose


Subject(s)
Carbohydrate Dehydrogenases/metabolism , Fungi/enzymology
3.
Arq. biol. tecnol ; 32(2): 377-90, jun. 1989. ilus
Article in English | LILACS | ID: lil-74928

ABSTRACT

With the purpose of elucidating the pathway of uridine-diphospate-N-acetyl-D-glucosamine formation in coffee plants, studies. These studies showed that UDP-N-acetyl-D-glucosamine is formed from fructose 6-phosphate and glutamine by a series of the following reactions: a) D-Glucosamine 6-P + acetylCoA N-acetul-D-Glucosamine 6-P ñ CoA c) N-Acetyl-D-glucosamine 6-P N-acetyl-D-glucosamine 1-P d) N-Acetyl-D-glucosamine 1-P + UTP UDP-N-acetyl-D-glucosaamine + PP Glucosamine 6-phospate was either obtained by its directly phosphorylation by ATP and hexokinase. Deaminase and phospatase activities were also determined


Subject(s)
Coffee , Uridine Diphosphate N-Acetylgalactosamine/biosynthesis
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