Electrophoretic and histochemical comparison of three strains of Aedes aegypti

Igbokwe, Emmanuel C.; Downe, A. E. R.

doi:10.1016/0305-0491(78)90117-7

Cited by 10 publications

(9 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Clear areas will indicate the presence of proteases after a period of 24 h. In order to determine the molecular weight (MW), 5 lL of Bio Basic Inc. BM523 commercial marker was placed in a small cup in each SDS-PAGE gel, which is made of the following proteins of molecular weight: rabbit phosphorilase B 97.4 KD, bovine serum albumin 66.2 KD, egg albumin 42.7 KD, carbonic anhydrase 31.0 KD and lysozyme 14.4 KD. The relative electromobility (Rf) was calculated for all zymograms (Igbokwe and Downe 1978), and MW of each band with alkaline protease activity was calculated with the linear adjustment between Rf and decadic logarithm of the molecular weights of the proteins used as markers and with the aid of Quantity One 1-D Analysis Software from Bio-Rad Ò .…”

Section: Electrophoretic Analysismentioning

confidence: 99%

Changes on digestive enzymes during initial ontogeny in the three-spot cichlid Cichlasoma trimaculatum

Toledo-Solís

Uscanga‐Martínez

Guerrero‐Zárate

et al. 2014

Fish Physiol Biochem

View full text Add to dashboard Cite

A study was performed in order to understand the development of digestive enzymes during initial ontogeny of Cichlasoma trimaculatum, for which the activity of acidic and alkaline proteases, lipases, amylases and phosphatases was determined by means of biochemical and electrophoretic analysis. Our results showed that the activity of alkaline proteases, trypsin and chymotrypsin is present from day 6 after hatching (dah) during exogenous feeding with Artemia nauplii. The activities of carboxypeptidase A and leucine aminopeptidase are present from the first days, increasing at 6 dah and reaching their maximum activity at 9 dah while acid protease activity started at 9 dah. Furthermore, the lipase activity is detected on 6 dah and keeps increasing and decreasing on 17 dah. Amylase activity is detected on 3 dah, presenting fluctuations until 45 dah, where it reaches its maximum activity. Acid and alkaline phosphatases are detected from 3 dah and reach a maximum activity between 13 and 19 dah. The SDS-PAGE electrophoresis revealed six types of bands in the alkaline proteases, with molecular weight between 113.4 and 20.4 kDa. First three bands appear on 6 dah, but it is until 11 dah when all isoforms appear. Based on these results, it is considered that this species completes its digestive enzymatic machinery from day 9 after hatching, therefore is recommended to perform the transition from live feed to inert feed at 15 dah.

show abstract

Section: Electrophoretic Analysismentioning

confidence: 99%

Changes on digestive enzymes during initial ontogeny in the three-spot cichlid Cichlasoma trimaculatum

Toledo-Solís

Uscanga‐Martínez

Guerrero‐Zárate

et al. 2014

Fish Physiol Biochem

View full text Add to dashboard Cite

show abstract

“…The LRMWM contained the following protein markers: phosphorylase b (97 kDa), serum bovine albumin (66 kDa), egg albumin (45 kDa), carbonic anhydrase (29 kDa), trypsinogen (24 kDa) and tryptic soy inhibitor (20 kDa). The relative electromobility (Rf) was calculated for all of the zymograms (Igbokwe & Downe, 1978), and the molecular weight (MW) of each band with alkaline protease activity was calculated as the lineal adjustment between Rf and the decimal logarithm of the molecular weights of the proteins used as markers using the software Quality One V 4.6.5 (Hercules, CA).…”

Section: Relative Migration Distance and Molecular Weight Calculationmentioning

confidence: 99%

Partial Characterization of Digestive Proteases in the Common Snook Centropomus undecimalis

Concha‐Frías¹,

Álvarez‐González²,

Gaxiola³

et al. 2016

IJB

View full text Add to dashboard Cite

Common snook (Centropomus undecimalis) is a marine species with high aquaculture potential; although its digestive physiology is still unknown and knowledge of that could allow the development of a balanced feed for commercial culture of this fish. The objective of this study was to partially characterize the digestive proteases in C. undecimalis using electrophoretic and biochemical techniques. A total of 50 wild snook juveniles were used to determine the optimal values of pH stability and temperature as well as the effect of inhibitors on digestive, gastric and intestinal proteases. The optimal pH for gastric proteases was obtained to be 2 with stability obtained between 2 and 8; the optimal temperature was detected at 75ºC for in vitro test, and the thermal stability was between 25 and 45ºC. Intestinal proteases showed two peaks of activity at a pH of 7 and 11; meanwhile, the greatest stability was found between a pH of 4 and 10; the optimal temperature was at 65ºC, and the greatest stability was detected between 35 and 45ºC. Up to 86% of the gastric protease activity was inhibited by pepstatin A; meanwhile, the intestinal proteases TPCK, TLCK, 1-10 Phenanthroline, SBT1, EDTA, PMSF and ovalbumin reduced the activity by 17%, 68%, 85%, 41%, 40.5%, 60% and 59%, respectively.

show abstract

“…The LRMWM contains the following proteins as markers: phosphorylase b (97 kDa), bovine serum albumin (66 kDa), egg albumin (45 kDa), carbonic anhydrase (29 kDa), trypsinogen (24 kDa), and soybean trypsic inhibitor (20 kDa). The relative electromobility (rf) was calculated for all the zymograms (Igbokwe and Downe 1978), and the molecular weight (MW) of each band with alkaline protease activity was calculated as the lineal adjustment between the Rf and the decimal logarithm of the molecular weights of the proteins used as markers, with Quality One V 4.6.5 software (Hercules, CA).…”

Section: Rf and Molecular Weight Calculationsmentioning

confidence: 99%

Changes in digestive enzyme activity during initial ontogeny of bay snook Petenia splendida

Uscanga‐Martínez

Perales‐García

Álvarez‐González

et al. 2011

Fish Physiol Biochem

View full text Add to dashboard Cite

Several samples of P. splendida larvae were obtained from eggs until day 60 after hatching (dah) to determine acid and alkaline proteases, trypsin, chymotrypsin, leucine aminopeptidase, α-amylase, lipase, and acid and alkaline phosphatase activities using biochemical techniques. Additionally, SDS-PAGE alkaline protease zymogram and PAGE acid protease zymogram were carried out to identify active isoforms during larviculture. Alkaline protease and chymotrypsin were present at the moment of hatching, increased gradually reaching the maximum values at 35 dah. Trypsin and leucine aminopeptidase activities were low from hatching, increasing gradually as larvae grew. Alkaline protease zymogram showed four zymogens, which appears at different days, remaining present until the end of the larviculture (95.2 kDa at 11 dah, 26.4 kDa at 9 dah, 21.4 kDa at 3 dah, and 23.3 kDa at hatching). Pepsin activity was present at day 7 after hatching and increased progressively until the end of the larviculture. Acid protease zymogram only showed one zymogen (0.65 rf), which appear at 6 dah. Lipase was high at the time of hatching and increased until 15 dah, after which decreased gradually. Amylase was high from the beginning and until 15 dah and then decreased rapidly to almost nothing onward. Alkaline and acid phosphatases presented a high activity at the egg stage, fell slightly during the first feeding and increased again from 20 to 30 dah. Results obtained in this study show that larvae can be fed artificial diets starting on day 10 after hatching.

show abstract

Electrophoretic and histochemical comparison of three strains of Aedes aegypti

Cited by 10 publications

References 18 publications

Changes on digestive enzymes during initial ontogeny in the three-spot cichlid Cichlasoma trimaculatum

Changes on digestive enzymes during initial ontogeny in the three-spot cichlid Cichlasoma trimaculatum

Partial Characterization of Digestive Proteases in the Common Snook Centropomus undecimalis

Changes in digestive enzyme activity during initial ontogeny of bay snook Petenia splendida

Contact Info

Product

Resources

About