scholarly journals Aminopeptidase activity is related to the amino acids composition of the food in passerine birds

2017 ◽  
Author(s):  
Cintia Garro ◽  
Antonio Brun ◽  
William Karasov ◽  
Enrique Caviedes-Vidal
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Feeding Habits ◽  
Adaptive Modulation ◽  
Aminopeptidase N ◽  
Enzyme Hydrolysis ◽  
The Other ◽  
Aminopeptidase Activity ◽  
Passerine Birds ◽  
Natural Diet

Background. Passerine birds exploit different kinds of feeding habits and they have to face seasonal changes in food availability. Therefore, the composition of the principal nutrient in their food differs from the usual. In consequence the digestive function – enzyme hydrolysis and absorption – have to adapt to these nutrients. These changes in digestive physiology could respond to the adaptive modulation hypothesis which postulated that the activities of digestive enzymes should match the levels of their substrates in their diet so energy is not wasted on enzymes that are no need. Thus, we decide to measure intestinal enzymes activities of two species of passerine birds that differ in natural diet. Overall we hypothesized that species with different feeding habits present enzyme activity according to the mainly component of the diet (e.g., carbohydrates, proteins). Our prediction is that the individuals will present enzyme activity proportionally to the primary components of the diets. Methods. We select for study: red ovenbirds (Furnarius rufus), which are strict insectivores and zebra finches (Taeniopygia guttata), which are specialist granivores. We complete the analysis with publish data for house sparrows (Passser domesticus) feed on high starch from the literature. To examine intestinal enzyme activities, we measured the activity of two disaccharidases (sucrase-isomaltase and maltase-glucoamilase) and one dipeptidase (aminopeptidase-N). Results. The average intestinal activity of sucrase shows that the omnivorous P. domesticus presents almost 4 times more activity than the granivorous T. guttata and more than 11 times than the insectivorous F. rufus. This difference is also reflected in the total sucrase hydrolytic capacity where P. domesticus has roughly 10 times more than the other two birds. Surprisingly in F. rufus we found maltase and aminopeptidase activity while sucrase activity was close to zero. In the case of the average activity of maltase for the omnivorous P. domesticus is approximately 40 % more than the granivorous T. guttata and more than 5 times than the insectivorous F. rufus. Although the total maltase hydrolytic capacity of P. domesticus is 5 times more than T. guttata and F. rufus. The average of aminopeptidase-N activity for F. rufus and T. guttata almost doubled the P. domesticus ones. Also F. rufus roughly doubles the other two birds in total aminopeptidase hydrolytic capacity. Discussion. This study has shown that exist a relationship between the levels of amino acids in the diet and the total aminopeptidase capacity, but in the case of carbohydrates this relationship is not evident.

scholarly journals Aminopeptidase activity is related to the amino acids composition of the food in passerine birds

2017 ◽  
Author(s):  
Cintia Garro ◽  
Antonio Brun ◽  
Enrique Caviedes-Vidal
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Feeding Habits ◽  
Adaptive Modulation ◽  
Aminopeptidase N ◽  
Enzyme Hydrolysis ◽  
The Other ◽  
Aminopeptidase Activity ◽  
Passerine Birds ◽  
Natural Diet

Background. Passerine birds exploit different kinds of feeding habits and they have to face seasonal changes in food availability. Therefore, the composition of the principal nutrient in their food differs from the usual. In consequence the digestive function – enzyme hydrolysis and absorption – have to adapt to these nutrients. These changes in digestive physiology could respond to the adaptive modulation hypothesis which postulated that the activities of digestive enzymes should match the levels of their substrates in their diet so energy is not wasted on enzymes that are no need. Thus, we decide to measure intestinal enzymes activities of two species of passerine birds that differ in natural diet. Overall we hypothesized that species with different feeding habits present enzyme activity according to the mainly component of the diet (e.g., carbohydrates, proteins). Our prediction is that the individuals will present enzyme activity proportionally to the primary components of the diets. Methods. We select for study: red ovenbirds (Furnarius rufus), which are strict insectivores and zebra finches (Taeniopygia guttata), which are specialist granivores. We complete the analysis with publish data for house sparrows (Passser domesticus) feed on high starch from the literature. To examine intestinal enzyme activities, we measured the activity of two disaccharidases (sucrase-isomaltase and maltase-glucoamilase) and one dipeptidase (aminopeptidase-N). Results. The average intestinal activity of sucrase shows that the omnivorous P. domesticus presents almost 4 times more activity than the granivorous T. guttata and more than 11 times than the insectivorous F. rufus. This difference is also reflected in the total sucrase hydrolytic capacity where P. domesticus has roughly 10 times more than the other two birds. Surprisingly in F. rufus we found maltase and aminopeptidase activity while sucrase activity was close to zero. In the case of the average activity of maltase for the omnivorous P. domesticus is approximately 40 % more than the granivorous T. guttata and more than 5 times than the insectivorous F. rufus. Although the total maltase hydrolytic capacity of P. domesticus is 5 times more than T. guttata and F. rufus. The average of aminopeptidase-N activity for F. rufus and T. guttata almost doubled the P. domesticus ones. Also F. rufus roughly doubles the other two birds in total aminopeptidase hydrolytic capacity. Discussion. This study has shown that exist a relationship between the levels of amino acids in the diet and the total aminopeptidase capacity, but in the case of carbohydrates this relationship is not evident.

scholarly journals Aminopeptidase activity is related to the amino acids composition of the food in passerine birds

2017 ◽  
Author(s):  
Cintia Garro ◽  
Antonio Brun ◽  
Enrique Caviedes-Vidal
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Feeding Habits ◽  
Adaptive Modulation ◽  
Aminopeptidase N ◽  
Enzyme Hydrolysis ◽  
The Other ◽  
Aminopeptidase Activity ◽  
Passerine Birds ◽  
Natural Diet

Background. Passerine birds exploit different kinds of feeding habits and they have to face seasonal changes in food availability. Therefore, the composition of the principal nutrient in their food differs from the usual. In consequence the digestive function – enzyme hydrolysis and absorption – have to adapt to these nutrients. These changes in digestive physiology could respond to the adaptive modulation hypothesis which postulated that the activities of digestive enzymes should match the levels of their substrates in their diet so energy is not wasted on enzymes that are no need. Thus, we decide to measure intestinal enzymes activities of two species of passerine birds that differ in natural diet. Overall we hypothesized that species with different feeding habits present enzyme activity according to the mainly component of the diet (e.g., carbohydrates, proteins). Our prediction is that the individuals will present enzyme activity proportionally to the primary components of the diets. Methods. We select for study: red ovenbirds (Furnarius rufus), which are strict insectivores and zebra finches (Taeniopygia guttata), which are specialist granivores. We complete the analysis with publish data for house sparrows (Passser domesticus) feed on high starch from the literature. To examine intestinal enzyme activities, we measured the activity of two disaccharidases (sucrase-isomaltase and maltase-glucoamilase) and one dipeptidase (aminopeptidase-N). Results. The average intestinal activity of sucrase shows that the omnivorous P. domesticus presents almost 4 times more activity than the granivorous T. guttata and more than 11 times than the insectivorous F. rufus. This difference is also reflected in the total sucrase hydrolytic capacity where P. domesticus has roughly 10 times more than the other two birds. Surprisingly in F. rufus we found maltase and aminopeptidase activity while sucrase activity was close to zero. In the case of the average activity of maltase for the omnivorous P. domesticus is approximately 40 % more than the granivorous T. guttata and more than 5 times than the insectivorous F. rufus. Although the total maltase hydrolytic capacity of P. domesticus is 5 times more than T. guttata and F. rufus. The average of aminopeptidase-N activity for F. rufus and T. guttata almost doubled the P. domesticus ones. Also F. rufus roughly doubles the other two birds in total aminopeptidase hydrolytic capacity. Discussion. This study has shown that exist a relationship between the levels of amino acids in the diet and the total aminopeptidase capacity, but in the case of carbohydrates this relationship is not evident.

Aminopeptidase Activity Profile in Cultured Human Osteoblasts

2011 ◽  
Vol 15 (1) ◽  
pp. 56-61 ◽  
Author(s):  
Gema Lucena ◽  
Candela Reyes-Botella ◽  
Olga García-Martínez ◽  
Lourdes Díaz-Rodríguez ◽  
Francisco Alba ◽  
...  
Keyword(s):  
Amino Acids ◽  
Bone Tissue ◽  
The Other ◽  
Aminopeptidase Activity ◽  
Cell Populations ◽  
Biological Processes ◽  
Activity Profile ◽  
Human Osteoblasts ◽  
Terminal Amino

Aminopeptidases (APs) are enzymes involved in a wide variety of biological processes and present in a variety of different cell populations. The authors studied these enzymes in primary cultured human osteoblasts in order to establish an activity profile and thereby contribute to knowledge of bone tissue. The authors used 13 different substrates ( N-terminal amino acids) and a fluorimetric assay to examine AP activity associated with the membranes of cultured osteoblasts. The authors demonstrated activity > 10 pmol/min/104 cells when glycine, alanine, leucine, arginine, phenylalanine, methionine, and lysine were used as substrates. The activity was markedly lower (<1.6 pmol/min/104 cells) when the other N-terminal amino acids were used. Puromycin and bestatin inhibited AP activity, though not completely, when we used AlaNA or LeuNA as substrates. Further studies are warranted to determine the role of these enzymes in bone tissue physiology.

Daily output of pancreatic juice and some dietary factors which influence it

1959 ◽  
Vol 197 (1) ◽  
pp. 27-30 ◽  
Author(s):  
D. F. Magee ◽  
S. S. Hong
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Casein Hydrolysate ◽  
Essential Amino Acids ◽  
Dietary Factors ◽  
The Other ◽  
Soy Flour ◽  
Mixed Diet ◽  
Daily Output ◽  
Milk Casein

Evidence is presented that the chronic pancreatic fistula dogs can be used effectively to study pancreatic physiology on a daily output basis. By increasing the amount of a mixed diet fed or by adding fat to the diet the volume and protease and lipase activities can be increased. Additions of cellulose, milk, casein hydrolysate were ineffective. On the basal mixed diet neither volume, amylase nor protease increased independently of each other. Changes in one enzyme activity without the other or in volume without enzymes were seen with supplements of essential amino acids or soy flour. The possible mechanism of these effects is discussed.

scholarly journals The metabolism of neuropeptides. Phase separation of synaptic membrane preparations with Triton X-114 reveals the presence of aminopeptidase N

1985 ◽  
Vol 231 (2) ◽  
pp. 445-449 ◽  
Author(s):  
R Matsas ◽  
S L Stephenson ◽  
J Hryszko ◽  
A J Kenny ◽  
A J Turner
Keyword(s):  
Phase Separation ◽  
Membrane Protein ◽  
Total Activity ◽  
Aminopeptidase N ◽  
The Other ◽  
Aminopeptidase Activity ◽  
Synaptic Membranes ◽  
Synaptic Membrane ◽  
Rich Phase ◽  
Triton X

The property of solutions of Triton X-114 to separate into detergent-rich and detergent-poor phases at 30 degrees C has been exploited to investigate the identities of the aminopeptidases in synaptic membrane preparations from pig striatum. When titrated with an antiserum to aminopeptidase N (EC 3.4.11.2), synaptic membranes solubilized with Triton X-100 revealed that this enzyme apparently comprises no more than 5% of the activity releasing tyrosine from [Leu]enkephalin. When assayed in the presence of puromycin, this proportion increased to 20%. Three integral membrane proteins were fractionated by phase separation in Triton X-114. Aminopeptidase activity, endopeptidase-24.11 and peptidyl dipeptidase A partitioned predominantly into the detergent-rich phase when kidney microvillar membranes were so treated. However, only 5.5% of synaptic membrane aminopeptidase activity partitioned into this phase, although the other peptidases behaved predictably. About half of the aminopeptidase activity in the detergent-rich phase could now be titrated with the antiserum, showing that aminopeptidase N is an integral membrane protein of this preparation. Three aminopeptidase inhibitors were investigated for their ability to discriminate between the different activities revealed by these experiments. Although amastatin was the most potent (IC50 = 5 × 10(−7) M) it failed to discriminate between pure kidney aminopeptidase N, the total activity of solubilized synaptic membranes and that in the Triton X-114-rich phase. Bestatin was slightly more potent for total activity (IC50 = 6.3 × 10(−6) M) than for the other two forms (IC50 = 1.6 × 10(−5) M). Puromycin was a weak inhibitor, but was more selective. The activity of solubilized membranes was more sensitive (IC50 = 1.6 × 10(−5) M) than that of the pure enzyme or the Triton X-114-rich phase (IC50 = 4 × 10(−4) M). We suggest that the puromycin-sensitive aminopeptidase activity that predominates in crude synaptic membrane preparations may be a cytosolic contaminant or peripheral membrane protein rather than an integral membrane component. Aminopeptidase N may contribute to the extracellular metabolism of enkephalin and other susceptible neuropeptides in the brain.

scholarly journals Digestive Enzymes in two Species of Marine Cinclodes (Passeriformes: Furnariidae)

The Condor ◽  
2003 ◽  
Vol 105 (4) ◽  
pp. 830-833
Author(s):  
Pablo Sabat ◽  
Sandra P. Gonzalez
Keyword(s):  
Enzyme Activity ◽  
Substrate Concentration ◽  
Digestive Enzymes ◽  
Digestive Enzyme ◽  
Aminopeptidase N ◽  
Digestive Enzyme Activity ◽  
Passerine Birds ◽  
Sucrase Activity ◽  
Frugivorous Birds ◽  
Prey Items

AbstractChanges in digestive enzyme activity along the intestine may be related to changes in substrate concentration in the intestine. We examined the distribution of digestive enzymes along the intestine in two species of carnivorous passerine birds from the genus Cinclodes. Both species lacked sucrase activity, suggesting that these species are unable to feed on sucrose-rich diets. Distribution of maltase and aminopeptidase-N activity differed from that found in other passerines, including omnivorous species, but resembled those found in herbivorous and frugivorous birds. We hypothesize that the type of prey items that Cinclodes consume may explain the pattern of maltase and aminopeptidase-N expression.Enzimas Digestivas en Dos Especies de Cinclodes Marinos (Passeriformes: Furnariidae)Resumen. Los cambios en los niveles de actividad enzimática digestiva a lo largo del intestino de aves pueden estar relacionados con cambios en la concentración de substratos en el intestino. En este estudio examinamos la distribución de enzimas digestivas a lo largo del intestino en dos especies de aves paseriformes del género Cinclodes. Ambas especies carecen de actividad de sacarasa lo que sugiere que estas especies son incapaces de consumir dietas ricas en sacarosa. La distribución de la actividad de maltasa y aminopeptidasa-N difiere de la documentada para otros paseriformes, incluyendo especies omnívoras, y es similar a la encontrada en aves herbívoras y frugívoras. Se sugiere que el tipo de presas consumidas por Cinclodes explicaría el patrón de expresión de maltasa y aminopeptidasa-N.

Genetic and environmental effects on the expression of peptidases and larval viability in Drosophila melanogaster.

Genetics ◽  
1992 ◽  
Vol 131 (3) ◽  
pp. 625-642 ◽  
Author(s):  
K Hiraizumi ◽  
P A Tavormina ◽  
K D Mathes
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Drosophila Melanogaster ◽  
Osmotic Stress ◽  
Genetic Background ◽  
Aminopeptidase Activity ◽  
Osmotic Concentration ◽  
Isogenic Lines ◽  
Activity Variation ◽  
Enzyme Activity Variation

Abstract The peptidase system in Drosophila melanogaster, consisting of dipeptidase-A, dipeptidase-B, dipeptidase-C and the leucine aminopeptidases, was used as a model to study the adaptive significance of enzyme activity variation. The involvement of the peptidases in osmoregulation has been suggested from the ubiquitous distribution of peptidase activities in nearly all tissues and the high concentration of amino acids and oligopeptides in the hemolymph. Under this hypothesis, larvae counteract increases in environmental osmotic stress by hydrolyzing peptides into amino acids both intra- and extracellularly to increase physiological osmotic concentration. The expression of the peptidases was studied by assaying for peptidase activities in third instar larvae of isogenic lines, which were reared under increasing levels of environmental osmotic stress using either D-mannitol or NaCl. Second and third chromosome substitution isogenic lines were used to assess the relative contribution of regulatory and structural genes in enzyme activity variation. Results indicate that: (1) genetic variation exists for peptidase activities, (2) the effect of osmotic stress is highly variable among peptidases, (3) changes in peptidase activities in response to osmotic stress depend on both genetic background and osmotic effector and (4) peptidase activities are correlated with each other, but these phenotypic correlations depend on genetic background, osmotic effector, and level of osmotic stress. Osmotic concentration in the larval hemolymph is correlated with leucine aminopeptidase activity, but changes in hemolymph osmotic concentration in response to environmental osmotic stress depend on the osmotic effector in the environment. Although these findings suggest that genetic and environmental factors contribute significantly toward the expression of enzymes with similar functions, a relative larval viability study of genotypes that differed significantly in dipeptidase-B (DIP-B) activity revealed that low DIP-B activity did not confer any measurable reduction in larval viability under increasing levels of environmental osmotic stress. These negative results suggest that, either DIP-B does not play a major role in osmoregulation or differential osmoregulation is not related to egg to adult viability in these tests.

TERATOGENIC EFFECT OF HERBICIDE GLIFONOX IN RATTUS NORVEGICUS, WISTAR STRAIN

2015 ◽  
Vol 8 ◽  
Author(s):  
Ricardo Ortiz Ortega ◽  
Karla S. Martínez Elizalde ◽  
Tomás Ernesto Villamar-Duque
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Rattus Norvegicus ◽  
Biological Material ◽  
Wistar Rats ◽  
Liver Enzymes ◽  
Teratogenic Effect ◽  
Transaminase Activity ◽  
Wistar Strain ◽  
Herbicide Glyphosate

<p>Teratogenic effect of herbicide glyphosate-Roundup, sold under the name Glifotox on Wistar rats was evaluated. The biological material was treated intraperitoneally with glyphosate at concentrations of 100, 125, and 150 mg/kg from gestation day nine. Hysterectomy was performed on day 18 of gestation, and the uterine horns where the embryos were located, in addition to recording the percentage of malformed embryos by modifying the method of Wilson were observed. The liver was removed and quantified by spectrophotometry with transaminase activity showed higher concentrations malformation rate and higher enzyme activity was 125 mg/kg, below is the average of 100 mg/kg and higher concentrations such as 150 mg/kg a large number of resorptions was obtained. It is concluded that glyphosate is toxic affecting the liver and liver enzymes involved in the formation of amino acids also produce delay in embryonic development.</p>

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