Chromatographic behavior of Bothrops erythromelas phospholipase and other venom constituents on Superdex 75

Preparative Biochemistry and Biotechnology

Volumn 34, Issue 4, 2004, Pages 345-364

  Aird, Steven D ^a,b  

^a FEDERAL UNIVERSITY OF PERNAMBUCO   (Brazil)

^b NORFOLK STATE UNIVERSITY   (United States)

Author keywords

Bothrops erythromelas; Buffer composition; Buffer pH; Calcium; Gel filtration chromatography; Phospholipase; Snake venom; Superdex 75

Indexed keywords

ION EXCHANGE RESIN; PHOSPHOLIPASE; SNAKE VENOM;

ANIMAL; ARTICLE; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; EVALUATION; GEL CHROMATOGRAPHY; ION EXCHANGE CHROMATOGRAPHY; ISOLATION AND PURIFICATION; METABOLISM; METHODOLOGY; PH; SNAKE;

ANIMALS; BOTHROPS; CHROMATOGRAPHY, AGAROSE; CHROMATOGRAPHY, ION EXCHANGE; CROTALID VENOMS; HYDROGEN-ION CONCENTRATION; ION EXCHANGE RESINS; PHOSPHOLIPASES;

BOTHROPS; BOTHROPS ERYTHROMELAS; NAJA; NAJA ATRA; SERPENTES;

EID: 7244243979     PISSN: 10826068     EISSN: None     Source Type: Journal    
DOI: 10.1081/PB-200030993     Document Type: Article

References (47)

1. Feitosa, R.F.; Melo, I.M.; Monteiro, H.S. Epidemiologia dos acidentes por serpentes peçonhentas no Estado do Ceará-Brasil. Rev. Soc. Bras. Med. Trop. 1997, 30, 295-301.
2. Kågedal, L.; Engström, B.; Ellegren, H.; Lieber, A.K.; Lundström, H.; Sköld, A.; Schenning, M. Chemical, physical and chromatographic properties of Superdex 75 prep grade and Superdex 200 prep grade gel filtration media. J. Chromatogr. 1991, 537, 17-32.
3. Drevin, I.; Johansson, B.L. Stability of Superdex 75 prep grade and Superdex 200 prep grade. J. Chromatogr. 1991, 547, 21-30.
4. Marinetti, G.V. The action of phospholipase A on lipoproteins. Biochim. Biophys. Acta 1965, 98 (3), 554-565.
5. 2 from Bothrops erythromelas (Viperidae: Jararaca Malha-de-Cascavel) venom, Proc. Reunião Científica Anual do Instituto Butantan, 4-8 dezembro de 2000, 2000; 131.
6. 2 from the venom of Agkistrodon halys pallas at 2.0 Å resolution. J. Mol. Biol. 1996, 255 (5), 669-676.
7. 2 from the venoms of rattlesnakes and other pit vipers. Arch. Biochem. Biophys. 2001, 394 (2), 236-244.
8. Acharya, A.S.; Di Donate, A.; Manjula, B.N.; Fischetti, V.A.; and Manning, J.M. Influence of trifluoroacetic acid on retention times of histidine-containing tryptic peptides in reverse phase HPLC. Int. J. Pept. Protein Res. 1983, 22, 78-82.
9. Bennett, H.P. Isolation of pituitary peptides by reversed-phase high-performance liquid chromatography. Expansion of the resolving power of reversed-phase columns by manipulating pH and the nature of the ion-pairing reagent. J. Chromatogr. 1983, 266, 501-510.
10. Guan, F.; Ishii, A.; Seno, H.; Watanabe-Suzuki, K.; Kumazawa, T.; Suzuki, O. Use of an ion-pairing reagent for high-performance liquid chromatography-atmospheric pressure chemical ionization mass spectrometry determination of anionic anticoagulant rodenticides in body fluids. J. Chromatogr. B. Biomed. Sci. Appl. 1999, 731, 155-165.
11. Janson, J.C. Adsorption phenomena on Sephadex. J. Chromatogr. 1967, 28 (1), 12-20.
12. Rendleman, J.A., Jr. Complexes of alkali metals and alkaline-earth metals with carbohydrates. Adv. Carbohydr. Chem. 1966, 21, 209-271.
13. Okada, T.; Miyakoshi, M.; Inoue, M. Adsorbability to and desorbability from Sephadex G-15 of sodium and phosphate ions. J. Chromatogr. 1989, 475, 412-415.
14. Egan, B.Z. Selectivity of polyacrylamide and dextran gels for simple cations and anions. J. Chromatogr. 1968, 34, 382-388.
15. Yoza, N.; Ogata, T.; Ohashi, S. The effect of sample concentration on the gel chromatographic behavior of alkaline earth metal ions on Sephadex columns. J. Chromatogr. 1970, 52, 329-338.
16. Ogata, T.; Yoza, N.; Ohashi, S. The effect of anions on the gel chromatographic behavior of magnesium ions. J. Chromatogr. 1971, 58, 267-276.
17. Yoza, N. Gel chromatography of inorganic compounds. J. Chromatogr. 1973, 86, 325-349.
18. Kura, G.; Koyama, A.; Tarutani, T. Chromatographic study of some inorganic ions on Sephadex gel in thiocyanate media. J. Chromatogr. 1977, 144, 245-252.
19. Richards, N.J.; Williams, D.G. Complex formation between aqueous zinc chloride and cellulose-related D-glucopyranosides. Carbohydr. Res. 1970, 12, 409-420.
20. Pharmacia LKB Biotechnology Gel Filtration. Principles and Methods, 5th Ed.; Rahms i Lund: Sweden, 1991; 102.
21. Morgan, R.S.; Morgan, N.H.; Guinavan, R.A. Zinc in Sephadex. Anal. Biochem. 1972, 45 (2), 668-669.
22. Klungsöyr, L. Quantitative estimation of protein. Separation of alkaline protein-copper complex from excess copper on Sephadex G-25. Anal. Biochem. 1969, 27 (1), 91-98.
23. Lowry, O.H.; Rosenbrough, N.J.; Fair, A.L.; Randall, R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 193 (1), 265-275.
24. Usher, D.J.; Deegan, T. An assessment of the use of Sephadex G-25 in the estimation of serum protein-bound magnesium and calcium. Clin. Chim. Acta 1970, 29(3), 361-367.
25. Gelotte, B. Studies on gel filtration. Sorption properties of the bed material Sephadex. J. Chromatogr. 1960, 3, 330-342.
26. Miranda, F.; Rochat, H.; Lissitzky, S. Propriétés éxchangeuses d'ions du gel de dextrane (Sephadex). Application à la mise au point d'une technique de rétention réversible des protéines basiques de faible poids moléculaire. J. Chromatogr. 1962, 7, 142-154.
27. Flodin, P. Molecular sieve effects in chromatography. Anal. Chim. Acta 1967, 38, 89-96.
28. Eaker, D.; Porath, J. Sorption effects in gel filtration: I. A survey of amino acid behavior on Sephadex G-10. Sep. Sci. 1967, 2 (4), 507-550.
29. Nedermeyer, P.A.; Rogers, L.B. Gel filtration behavior of inorganic salts. Anal. Chem. 1968, 40, 755-762.
30. Reed, K.C. Binding of calcium by cellulose membranes and Sephadex. Biochem. Biophys. Res. Commun. 1973, 50 (4), 1136-1142.
31. Rothenbühler, E.; Waibel, R.; Solms, J. An improved method for the separation of peptides and α-amino acids on copper-Sephadex. Anal. Biochem. 1979, 97 (2), 367-375.
32. Later, R.; Quincy, C. Méthode sensible de détection en continu des peptides et des protéines par la réaction du Biuret utilisant un reacteur cuivre-Sephadex. J. Chromatogr. 1979, 174 (1), 131-141.
33. Drevin, I.; Larsson, L.; Eriksson, I.; Johansson, B.L. Chemical properties of and solute-support interactions with the gel filtration medium Superdex 75 prep grade. J. Chromatogr. 1990, 514, 137-146.
34. Porath, J. Some recently developed fractionation procedures and their application to peptide and protein hormones. Pure Appl. Chem. 1960, 6, 233-244.
35. Porath, J. Gel filtration of proteins, peptides and amino acids. Biochim. Biophys. Acta 1960, 39, 193-207.
36. Bretthauer, R.K.; Golichowski, A.M. Adsorption chromatography of phenylalanine peptides on Sephadex. Biochim. Biophys. Acta 1967, 155 (2), 549-557.
37. Determann, H.; Walter, I. Source of aromatic affinity to 'Sephadex' dextran gels. Nature 1968, 219 (154), 604-605.
38. 2 for the venom of Agkistrodon halys blomhoffii at 2.8 Å resolution. Biochem. Biophys. Res. Comm. 1992, 184, 137-143.
39. Guo, Y.W.; Chen, C.T.; Chang, T.Y. Cloning and functional expression of an edema-producing factor from Trimeresurus mucrosquamatus. NCBI Accession #AAK97534 2001; unpublished sequence.
40. 2 from the venom of Deinagkistrodon acutus. Acta Crystallogr. D. Biol. Crystallogr. 2002, 58 (1), 104-110.
41. Ferreira, S.H.; Bartelt, D.C.; Greene, L.J. Isolation of bradykinin-potentiating peptides from Bothrops jararaca venom. Biochemistry 1970, 9 (13), 2583-2593.
42. Kato, H.; Suzuki, T. Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffi. Isolation of five bradykinin potentiators and the amino acid sequences of two of them, potentiators B and C. Biochemistry 1971, 10 (6), 972-980.
43. Ondetti, M.A.; Williams, N.J.; Sabo, E.F.; Pluscec, J.; Weaver, E.R.; Kocy, O. Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis. Biochemistry 1971, 10 (22), 4033-4039.
44. Greene, L.J.; Camargo, A.C.; Krieger, E.M.; Stewart, J.M.; Ferreira, S.H. Inhibition of the conversion of angiotensin I to II and potentiation of bradykinin by small peptides present in Bothrops jararaca venom. Circ. Res. 1972, 31 (Suppl. 2), 62-71.
45. Chi, C.W.; Wang, S.Z.; Xu, L.G.; Wang, M.Y.; Lo, S.S.; Huang, W.D. Structure-function studies on the bradykinin potentiating peptide from Chinese snake venom (Agkistrodon halys Pallas). Peptides 1985, 6 (Suppl. 3), 339-342.
46. Murayama, N.; Hayashi, M.A.F.; Ohi, H.; Ferreira, L.A.F.; Hermann, V.V.; Saito, H.; Fujita, Y.; Higuchi, S.; Fernandes, B.L.; Yamane, T.; de Camargo, A.C.M. Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide. Proc. Natl. Acad. Sci. USA 1997, 94 (4), 1189-1193.
47. Bjarnason, J.B.; Fox, J.W. Hemorrhagic metalloproteinases from snake venoms. Pharm. Ther. 1994, 62 (3), 325-372.