In this work, we describe antibacterial peptides from Hadruroides mauuryi and Centruroides margaritatus scorpion venom, isolated by ionic exchange chromatography with 0,05M ammonium acetate buffer pH 7. H. mauryi venom (44,4 mg) was separated in 7 protein peaks. IV peak inhibited growth of Escherichia coli, Pseudomona aeuginosa and Bacillus cereus: V peak affect to P. aeruginosa and B. cereus, and VI peak have activity on B. cereus. C. margaritatus venom (50,6 mg) was also separated en 7 protein peaks. II peak inhibited growth of Staphylococcus aureus; III, IV, V and VI peaks affect to S. aureus , P. aeruginosa and B. cerus; and finally VII peak affect to P. aeruginosa. All isolated peptides were of basic pH, with exception of II peak from C. margaritatus. In addition, all peptides have not hemolitic activity.

Hl3 is a toxin isolated by our investigation group from Hadruroides lunatus scorpion venom by ionexchange chromatography on CM-Sephadex C-25 to pH 7, and which produce contraction and paralysis in the inoculated limb of white mice. In this work we have determined that inoculation of Hl3 (26 μg) in gastrocnemius muscle from mice produces the release in plasma of creatine kinase and lactate deshidrogenase. The creatine kinase activity increases from 210 UI/L to 8015 UI/L in 60 minutes, whrereas the LDH activity increases from 174 UI/L to 1697 UI/L in 90 minutes. By PAGE-SDS it, was demonstrated that incubation of Hl3 with gastrocnemius muscle isolated from white mice, in physiological solution to pH 7, produces the release of other different muscular proteins as well. In addition Hl3 can increase the calcium intramuscular 3,5 fold, after 45 minutes of action. Our results suggest that Hl3 ...

Proteins of Centruroides margaritatus scorpion venom had been separated by cationic exchange chromatography in CM-Sephadex C-25 with 0,05M ammonium acetate pH 7, from 28,3 mg of venom obtained from 52 adults scorpions caught in Zarumilla, Tumbes, north of Peru. The chromatographic elution showed 9 protein peaks and toxicity assays allowed the identification of three toxins with specific activity on crustacean, insects and rodents, respectively. Both the crude venom and the collected fractions have shown neither phospholipase nor proteoyitic activity. The PAGE-SDS of crude venom shows one very notorious protein band of 14 kDa aproximately, and another two thin bands of 45 kDa aproximately, which imply that the majority of proteins from this venom are of a molecular weight similar or less than 14kDa.

The proteins from the venom of the scorpion Hadruroides lunatus were separated by ionexchange chromatography on CM-Sephadex C-25 with 0,05M ammonium acetate buffer pH 7, getting six protein peaks in the process. The toxicity tests allowed the identification of three toxins that were denominated Hl1, Hl2 y Hl3; which immobilize, respectively, insects (Grillus sp.), crustaceans (Porcellio laevis) and the inoculated limb of white mice. The three toxins are basic proteins and have no proteolitic or phospholipase activity. In addition, Hl3 increases the plasmatic level of creatine kinase after its inoculation in the gastrocnemius muscle of mice. By PAGE-SDS, Hl3 shows only one protein band of 12,5 KDa, while the other toxins have protein contaminants.

The biochemistry of the venom of Tityus kaderkai Kovařik, 2005 from Madre de Dios department, has been studied. The soluble venom contains 47.6% of protein. The venom proteins were separated from 12.9 mg of venom using cationic exchange chromatography in CM Sephadex C-25 with a 0.05 M ammonium acetate buffer pH 7.0. The chromatography profiles show seven peaks of proteins (I – VII) and five protein bands were distinguished in the crude venom, by PAGE-SDS. The toxicity assays allowed the identification of three toxins affecting Mus musculuswhich were associated to peaks IV, V and VII. Toxic proteins to Gryllus sp. were also found associated to peaks IV, V, VI and VII. Through the enzymatic activity, the presence of proteolytic activity over casein was found related to the first peak. Hyaluronidase activity has also been found in the peak IV with a specific activity 205.6 μg/min/mg. Ho...

En este trabajo se describen algunos péptidos antibacterianos de los venenos de los escorpiones Hadruroides mauryi (Francke y Soleglad, 1980) y Centruroides margaritatus (Gervais, 1841), aislados mediante cromatografía de intercambio iónico en CM Sephadex C-25 con buffer acetato de amonio 0,05M a pH 7. El veneno de H. mauryi (44,4 mg) fue separado en 7 fracciones proteicas. La fracción IV inhibió el crecimiento de Escherichia coli, Pseudomona aeuginosa y Bacillus cereus; la fracción V afectó a P. aeruginosa y B. cereus; y fracción VI mostró actividad sobre B. cereus. El veneno de C. margaritatus (50,6 mg) también fue fraccionado en 7 fracciones proteicas. La fracción II inhibió el crecimiento de Staphylococcus aureus; Las fracciones III, IV, V y VI afectaron a S. aureus, P. aeruginosa y B. cereus; y finalmente la fracción VII afectó a P. aeruginosa. En todos los casos los p...

Hl3 is a toxin isolated by our investigation group from Hadruroides lunatus scorpion venom by ionexchange chromatography on CM-Sephadex C-25 to pH 7, and which produce contraction and paralysis in the inoculated limb of white mice. In this work we have determined that inoculation of Hl3 (26 μg) in gastrocnemius muscle from mice produces the release in plasma of creatine kinase and lactate deshidrogenase. The creatine kinase activity increases from 210 UI/L to 8015 UI/L in 60 minutes, whrereas the LDH activity increases from 174 UI/L to 1697 UI/L in 90 minutes. By PAGE-SDS it, was demonstrated that incubation of Hl3 with gastrocnemius muscle isolated from white mice, in physiological solution to pH 7, produces the release of other different muscular proteins as well. In addition Hl3 can increase the calcium intramuscular 3,5 fold, after 45 minutes of action. Our results suggest that Hl3 ...

Las proteínas del veneno del escorpión Centruroides margaritatus, fueron separadas mediante cromatografía de intercambio catiónico en CM-Sephadex C-25 con buffer acetato de amonio 0,05M a pH 7, a partir de 28,3 mg de veneno obtenidos de 52 ejemplares adultos capturados en la provincia de Zarumilla, Tumbes, norte del Perú. El perfil cromatográfico mostró la presencia de 9 picos de proteína y los ensayos de toxicidad han permitido identificar tres tipos de toxinas, cada una específica para crustáceos, insectos y roedores, respectivamente. Tanto en el veneno crudo como en las fracciones colectadas, no se encontró actividad de fosfolipasa ni actividad proteolítica. La PAGE-SDS del veneno crudo, muestra la presencia de una banda bastante notoria de aproximadamente 14 KDa, y otras dos muy tenues, de aproximadamente 45KDa, lo cual significa que la mayoría de proteínas de este vene...

The proteins from the venom of the scorpion Hadruroides lunatus were separated by ionexchange chromatography on CM-Sephadex C-25 with 0,05M ammonium acetate buffer pH 7, getting six protein peaks in the process. The toxicity tests allowed the identification of three toxins that were denominated Hl1, Hl2 y Hl3; which immobilize, respectively, insects (Grillus sp.), crustaceans (Porcellio laevis) and the inoculated limb of white mice. The three toxins are basic proteins and have no proteolitic or phospholipase activity. In addition, Hl3 increases the plasmatic level of creatine kinase after its inoculation in the gastrocnemius muscle of mice. By PAGE-SDS, Hl3 shows only one protein band of 12,5 KDa, while the other toxins have protein contaminants.

The biochemistry of the venom of Tityus kaderkai Kovařik, 2005 from Madre de Dios department, has been studied. The soluble venom contains 47.6% of protein. The venom proteins were separated from 12.9 mg of venom using cationic exchange chromatography in CM Sephadex C-25 with a 0.05 M ammonium acetate buffer pH 7.0. The chromatography profiles show seven peaks of proteins (I – VII) and five protein bands were distinguished in the crude venom, by PAGE-SDS. The toxicity assays allowed the identification of three toxins affecting Mus musculuswhich were associated to peaks IV, V and VII. Toxic proteins to Gryllus sp. were also found associated to peaks IV, V, VI and VII. Through the enzymatic activity, the presence of proteolytic activity over casein was found related to the first peak. Hyaluronidase activity has also been found in the peak IV with a specific activity 205.6 μg/min/mg. Ho...

La investigación presentada tuvo como objetivo general analizar cómo es el proceso de contratación de régimen especial en un organismo regulador de Lima, 2023. El estudio se elaboró con un enfoque cualitativo de tipo básico y utilizó como diseño de investigación el estudio de caso, cuyo escenario fue un organismo regulador que tiene como competencias la supervisión de las actividades de energía y minería, siendo la técnica utilizada una entrevista semiestructurada y el instrumento un guión de 15 preguntas, aplicada a 14 participantes. Como resultado se observaron 7 coeficientes de co-ocurrencia cuyos valores fueron de 0.74, 0.73, 0.71, 0.68, 0.63, 0.59 y 0.52, que están asociadas a las cinco subcategorías previamente planteadas: actuaciones iniciales, proceso de selección, ejecución del contrato, alcance y limitaciones, confirmándose lo formulado para dichas subcategor...

By means of cationic exchange chromatography on CM-Sephadex C-25 column (16 x 1,1 cm) with ammonium acetate buffer 0,05 M at pH 7, from Brachistosternus ehrenbergii scorpion venom was isolated a protein with toxic activity on mice. In this system the toxin was ligated to gel and was eluated with buffer and NaCl 0,6M. The toxin denominated Be1 and it characterizes to be a basic protein that constitute 8,1% of venom total protein. Toxin purity was evaluated by electrophoresis in natives conditions, according to Reisfeld-method, and denaturants conditions by the Schägger-and-von Jagow-method, the toxin is a single chain polypeptide of 6,3 kDa has been determined. The inoculation of 60 μg toxin on albino mice, intraperitoneal way, produces some local signals as salival hipersecretion followed by respiratory affection, drags hind feet and finally 2 hours after, death. Intramuscular way (7,6...

A toxin (Hm3) was purified from the scorpion venom Hadruroides mauryi, by ion-exchange chromatography on CM-Sephadex C-25 with 0,05M ammonium acetate buffer pH 7. The toxin produce contraction and immobilize the inoculated limb of white mice, and is a basic protein with a molecular weight of 4,5 kDa. After of 45 minutes inoculated in gastrocnemius muscle of white mice, Hm3 (30,4 µg) increases the plasmatic level of creatine kinase from 252,6 UI/L to 3779,3 UI/L and lactate deshidrogenase from 142,7 UI/L to 248,2 UI/L; likewise increases the level of intramuscular calcium from 34,1 nmoles to 69,3 nmoles. This toxin have not proteolitic or phospholipase activity.

In this work, the poison of Phymactis papillosa collected in Ancón bay has been studied biochemically. The venom was obtained by hypotonic shock and then lyophilized. Electrophoretic analysis of the soluble poison showed the presence of 5 protein bands with molecular weights between 5 and 25.1 kDa.The soluble venom was fractionated by filtration chromatography on a Sephadex G-50 column, yielding four protein peaks (I, II, III and IV). In the soluble venom and collected fractions was measured protease activity, phospholipase, hyaluronidase, acid phosphatase and alkaline phosphatase; as well as hemolytic and neurotoxic activity. Proteolytic activity on casein was found in the soluble venom and peaks I and III. Was not detected phospholipase activity, hyaluronidase, acid phosphatase and alkaline phosphatase. Hemolytic activity on human red cells tested, was found in the soluble venom and p...

By means of cationic exchange chromatography on CM-Sephadex C-25 column (16 x 1,1 cm) with ammonium acetate buffer 0,05 M at pH 7, from Brachistosternus ehrenbergii scorpion venom was isolated a protein with toxic activity on mice. In this system the toxin was ligated to gel and was eluated with buffer and NaCl 0,6M. The toxin denominated Be1 and it characterizes to be a basic protein that constitute 8,1% of venom total protein. Toxin purity was evaluated by electrophoresis in natives conditions, according to Reisfeld-method, and denaturants conditions by the Schägger-and-von Jagow-method, the toxin is a single chain polypeptide of 6,3 kDa has been determined. The inoculation of 60 μg toxin on albino mice, intraperitoneal way, produces some local signals as salival hipersecretion followed by respiratory affection, drags hind feet and finally 2 hours after, death. Intramuscular way (7,6...

A toxin (Hm3) was purified from the scorpion venom Hadruroides mauryi, by ion-exchange chromatography on CM-Sephadex C-25 with 0,05M ammonium acetate buffer pH 7. The toxin produce contraction and immobilize the inoculated limb of white mice, and is a basic protein with a molecular weight of 4,5 kDa. After of 45 minutes inoculated in gastrocnemius muscle of white mice, Hm3 (30,4 µg) increases the plasmatic level of creatine kinase from 252,6 UI/L to 3779,3 UI/L and lactate deshidrogenase from 142,7 UI/L to 248,2 UI/L; likewise increases the level of intramuscular calcium from 34,1 nmoles to 69,3 nmoles. This toxin have not proteolitic or phospholipase activity.

En este trabajo se ha estudiado bioquímicamente el veneno de Phymactis papillosa, colectadas en la bahía de Ancón. El veneno fue obtenido mediante shock hipotónico y luego se liofilizó. El análisis electroforético del veneno soluble mostró la presencia de 5 bandas proteicas con pesos moleculares entre 5 y 25.1 kDa.El veneno soluble fue fraccionado por cromatografía de filtración en una columna de Sephadex G-50, obteniéndose cuatro picos de proteína (I, II, III y IV). Tanto en el veneno soluble como en las fracciones colectadas se midió actividad de proteasa, fosfolipasa, hialuronidasa, fosfatasa ácida y fosfatasa alcalina; así como, actividad hemolítica y neurotóxica. Se encontró actividad proteolítica sobre caseína, en el veneno soluble y en los picos I y III. No se detectó actividad de fosfolipasa, hialuronidasa, fosfatasa ácida y fosfatasa alcalina. La actividad ...

A myotoxin from Bothrops atrox snake venom was purified by cationic exchange on CM-Sephadex C-50 with 0,05M ammonium acetate pH 7. The myotoxin is a basic protein and by gel filtration and PAGE-SDS was demonstrated that protein has a molecular weight of 27 kDa and two polipeptides chain of 14 kDa each one. The inoculation of myotoxin in gastrocnemius muscle of white mice produce liberation of creatin kinase as well as myonecrosis. The myotoxin has phospholipasic, anticoagulant and edematic activity, but not hemolytic activity.

The myotoxin isolated from the venom of the snake Bothrops brazili has been studied in its mode of action. In the first hour of activity the myotoxin injected in the gastrocnemius muscle of white mice, induces the release of creatine kinase and lactate dehydrogenase, while by PAGE-SDS, it is shown that the incubation of miotoxin with isolated gastrocnemius muscle releases other proteins from this tissue. Moreover myotoxin produces hipercontraction, delta lesions and increases the concentration of intramuscular calcium “in vivo” and “in vitro”, which does not depend on extracellular calcium entry through dyhidropyridine receptors. This increase of calcium would explain the hipercontraction observed. Also it could trigger the activation of endogenous proteases and lipases, which would lead to muscle necrosis.

A myotoxin from the venom of the snake Bothrops brazili has been purified by ion-exchange chromatography on CM-Sephadex C-50 with 0,05 M ammonium acetate buffer pH 7. The homogeneity was evaluated by PAGE with and without SDS, immunodiffusion and immunoelectrophoresis. The myotoxin is a basic protein with 15,6% of Lys+Arg; it is not a glicoprotein, has not enzymatic activity, and corresponds to 25% of the whole venom protein. The molecular weight of the myotoxin was determined by PAGE-SDS and gel filtration chromatography. The myotoxin has 30 KDa of molecular weight and two polypeptide chains of 15 KDa each. Myotoxin produces a severe necrosis on the gastrocnemius muscle of white mice. The myotoxin does not have hemolytic nor anticoagulant activity. However, produces edema with a DEM of 32,6 mg of protein.