scholarly journals Two phospholipase A2 inhibitors from the plasma of Cerrophidion (Bothrops) godmani which selectively inhibit two different group-II phospholipase A2 myotoxins from its own venom: isolation, molecular cloning and biological properties

2000 ◽  
Vol 346 (3) ◽  
pp. 631-639 ◽  
Author(s):  
Sergio LIZANO ◽  
Yamileth ANGULO ◽  
Bruno LOMONTE ◽  
Jay W. FOX ◽  
Gérard LAMBEAU ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Biological Properties ◽  
Amino Acid Sequence Analysis ◽  
Terminal Amino Acid ◽  
Phospholipases A2 ◽  
Terminal Amino ◽  
Group Ii ◽  
Inhibition Studies ◽  
Phospholipase A2 Inhibitors ◽  
Insight Into

Myotoxic phospholipases A2 (PLA2s; group II) account for most of the muscle-tissue damage that results from envenomation by viperid snakes. In the venom of the Godman's viper (Cerrophidion godmani, formerly Bothrops godmani), an enzymically active PLA2 (myotoxin I) and an inactive, Lys-49 variant (myotoxin II) induce extensive muscle damage and oedema. In this study, two distinct myotoxin inhibitor proteins of C. godmani, CgMIP-I and CgMIP-II, were purified directly from blood plasma by selective binding to affinity columns containing either myotoxin I or myotoxin II, respectively. Both proteins are glycosylated, acidic (pI = 4) and composed of 20-25-kDa subunits that form oligomers of 110 kDa (CgMIP-I) or 180 kDa (CgMIP-II). In inhibition studies, CgMIP-I specifically neutralized the PLA2 and the myotoxic, oedema-forming and cytolytic activities of myotoxins I, whereas CgMIP-II selectively inhibited the toxic properties of myotoxin II. N-terminal amino acid sequence analysis and sequencing of cDNAs encoding the two inhibitors revealed that CgMIP-I is similar to γ-type inhibitors, which share a pattern of cysteine residues present in the Ly-6 superfamily of proteins, whereas CgMIP-II shares sequence identity with α-type inhibitors that contain carbohydrate-recognition-like domains, also found in C-type lectins and mammalian PLA2 receptors. N-terminal sequencing of myotoxin I revealed a different primary structure from myotoxin II [De Sousa, Morhy, Arni, Ward, Díaz and Gutiérrez (1998) Biochim. Biophys. Acta 1384, 204-208], which provides insight into the nature of such pharmacological specificity.

scholarly journals A New Group II Phospholipase A2 from Walterinnesia aegyptia Venom with Antimicrobial, Antifungal, and Cytotoxic Potential

Processes ◽  
2020 ◽  
Vol 8 (12) ◽  
pp. 1560
Author(s):  
Islem Abid ◽  
Ikram Jemel ◽  
Mona Alonazi ◽  
Abir Ben Bacha
Keyword(s):  
Phospholipase A2 ◽  
Snake Venom ◽  
Specific Activity ◽  
Industrial Effluents ◽  
Phospholipases A2 ◽  
Microbial Infections ◽  
Snake Venom Phospholipase ◽  
Terminal Amino ◽  
Group Ii ◽  
Cancerous Cells

Many venomous species, especially snakes, contain a variety of secreted phospholipases A2 that contribute to venom toxicity and prey digestion. We characterized a novel highly toxic phospholipase A2 of group II, WaPLA2-II, from the snake venom of Saudi Walterinnesia aegyptia (W. aegyptia). The enzyme was purified using a reverse phase C18 column. It is a monomeric protein with a molecular weight of approximately 14 kDa and an NH2-terminal amino acid sequence exhibiting similarity to the PLA2 group II enzymes. WaPLA2-II, which contains 2.5% (w/w) glycosylation, reached a maximal specific activity of 1250 U/mg at pH 9.5 and 55 °C in the presence of Ca2+ and bile salts. WaPLA2-II was also highly stable over a large pH and temperature range. A strong correlation between antimicrobial and indirect hemolytic activities of WaPLA2 was observed. Additionally, WaPLA2-II was found to be significantly cytotoxic only on cancerous cells. However, chemical modification with para-Bromophenacyl bromide (p-BPB) inhibited WaPLA2-II enzymatic activity without affecting its antitumor effect, suggesting the presence of a separate ‘pharmacological site’ in snake venom phospholipase A2 via its receptor binding affinity. This enzyme is a candidate for applications including the treatment of phospholipid-rich industrial effluents and for the food production industry. Furthermore, it may represent a new therapeutic lead molecule for treating cancer and microbial infections.

scholarly journals Factor D̄ of the alternative pathway of human complement. Purification, alignment and N-terminal amino acid sequences of the major cyanogen bromide fragments, and localization of the serine residue at the active site

1980 ◽  
Vol 187 (3) ◽  
pp. 863-874 ◽  
Author(s):  
D M Johnson ◽  
J Gagnon ◽  
K B Reid
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Alternative Pathway ◽  
Amino Acid Sequences ◽  
Serine Residue ◽  
Amino Acid Sequence Analysis ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

The serine esterase factor D of the complement system was purified from outdated human plasma with a yield of 20% of the initial haemolytic activity found in serum. This represented an approx. 60 000-fold purification. The final product was homogeneous as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis (with an apparent mol.wt. of 24 000), its migration as a single component in a variety of fractionation procedures based on size and charge, and its N-terminal amino-acid-sequence analysis. The N-terminal amino acid sequence of the first 36 residues of the intact molecule was found to be homologous with the N-terminal amino acid sequences of the catalytic chains of other serine esterases. Factor D showed an especially strong homology (greater than 60% identity) with rat ‘group-specific protease’ [Woodbury, Katunuma, Kobayashi, Titani, & Neurath (1978) Biochemistry 17, 811-819] over the first 16 amino acid residues. This similarity is of interest since it is considered that both enzymes may be synthesized in their active, rather than zymogen, forms. The three major CNBr fragments of factor D, which had apparent mol.wts. of 15 800, 6600 and 1700, were purified and then aligned by N-terminal amino acid sequence analysis and amino acid analysis. By using factor D labelled with di-[1,3-14C]isopropylphosphofluoridate it was shown that the CNBr fragment of apparent mol.wt. 6600, which is located in the C-terminal region of factor D, contained the active serine residue. The amino acid sequence around this residue was determined.

scholarly journals N-terminal amino acid sequence analysis of the subunits of pea photosystem I

FEBS Letters ◽  
1988 ◽  
Vol 228 (1) ◽  
pp. 157-161 ◽  
Author(s):  
Paul P.J. Dunn ◽  
Leonard C. Packman ◽  
Darryl Pappin ◽  
John C. Gray
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Photosystem I ◽  
Amino Acid Sequence Analysis ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

scholarly journals Mononuclear gold(iii) complexes withl-histidine-containing dipeptides: tuning the structural and biological properties by variation of the N-terminal amino acid and counter anion

2017 ◽  
Vol 46 (8) ◽  
pp. 2594-2608 ◽  
Author(s):  
Beata Warżajtis ◽  
Biljana Đ. Glišić ◽  
Nada D. Savić ◽  
Aleksandar Pavic ◽  
Sandra Vojnovic ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biological Properties ◽  
Counter Anion ◽  
Terminal Amino Acid ◽  
Terminal Amino

Gold(iii) complexes withl-Ala-l-His andl-Leu-l-His dipeptides inhibit angiogenesis.

scholarly journals Identification, description and structural analysis of beta phospholipase A2 inhibitors (sbβPLIs) from Latin American pit vipers indicate a binding site region for basic snake venom phospholipases A2

Toxicon X ◽  
2019 ◽  
Vol 2 ◽  
pp. 100009
Author(s):  
Consuelo Latorre Fortes-Dias ◽  
Carlos Alexandre H. Fernandes ◽  
Paula Ladeira Ortolani ◽  
Patrícia Cota Campos ◽  
L.A. Melo ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Phospholipase A2 ◽  
Binding Site ◽  
Latin American ◽  
Snake Venom ◽  
Phospholipases A2 ◽  
Phospholipase A2 Inhibitors

scholarly journals Characterization of Serracin P, a Phage-Tail-Like Bacteriocin, and Its Activity against Erwinia amylovora, the Fire Blight Pathogen

2002 ◽  
Vol 68 (11) ◽  
pp. 5704-5710 ◽  
Author(s):  
Abdelhamid Jabrane ◽  
Ahmed Sabri ◽  
Philippe Compère ◽  
Philippe Jacques ◽  
Isabel Vandenberghe ◽  
...  
Keyword(s):  
Fire Blight ◽  
Erwinia Amylovora ◽  
Culture Supernatant ◽  
Bacterial Disease ◽  
Amino Acid Sequence Analysis ◽  
Terminal Amino Acid ◽  
Phage Tail ◽  
Terminal Amino ◽  
Pear Trees

ABSTRACT Serratia plymithicum J7 culture supernatant displayed activity against many pathogenic strains of Erwinia amylovora, the causal agent of the most serious bacterial disease of apple and pear trees, fire blight, and against Klebsiella pneumoniae, Serratia liquefaciens, Serratia marcescens, and Pseudomonas fluorescens. This activity increased significantly upon induction with mitomycin C. A phage-tail-like bacteriocin, named serracin P, was purified from an induced culture supernatant of S. plymithicum J7. It was found to be the only compound involved in the antibacterial activity against sensitive strains. The N-terminal amino acid sequence analysis of the two major subunits (23 and 43 kDa) of serracin P revealed high homology with the Fels-2 prophage of Salmonella enterica, the coliphages P2 and 168, the φCTX prophage of Pseudomonas aeruginosa, and a prophage of Yersinia pestis. This strongly suggests a common ancestry for serracin P and these bacteriophages.

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